Enzyme Nomenclature

EC 2.3.1 (continued)

Acyltransferases

Continued from:
EC 2.3.1.1 to EC 2.3.1.50
EC 2.3.1.51 to EC 2.3.1.100
EC 2.3.1.101 to EC 2.3.1.150
EC 2.3.1.151 to EC 2.3.1.200

Contents

EC 2.3.1.201 UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
EC 2.3.1.202 UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
EC 2.3.1.203 UDP-N-acetylbacillosamine N-acetyltransferase
EC 2.3.1.204 octanoyl-[GcvH]:protein N-octanoyltransferase
EC 2.3.1.205 fumigaclavine B O-acetyltransferase
EC 2.3.1.206 3,5,7-trioxododecanoyl-CoA synthase
EC 2.3.1.207 β-ketodecanoyl-[acyl-carrier-protein] synthase
EC 2.3.1.208 4-hydroxycoumarin synthase
EC 2.3.1.209 dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
EC 2.3.1.210 dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
EC 2.3.1.211 bisdemethoxycurcumin synthase
EC 2.3.1.212 benzalacetone synthase
EC 2.3.1.213 cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6'''-O-hydroxycinnamoyltransferase
EC 2.3.1.214 pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4'''-malonyltransferase
EC 2.3.1.215 anthocyanidin 3-O-glucoside 6''-O-acyltransferase
EC 2.3.1.216 5,7-dihydroxy-2-methylchromone synthase
EC 2.3.1.217 curcumin synthase
EC 2.3.1.218 phenylpropanoylacetyl-CoA synthase
EC 2.3.1.219 demethoxycurcumin synthase
EC 2.3.1.220 2,4,6-trihydroxybenzophenone synthase
EC 2.3.1.221 noranthrone synthase
EC 2.3.1.222 phosphate propanoyltransferase
EC 2.3.1.223 3-oxo-5,6-didehydrosuberyl-CoA thiolase
EC 2.3.1.224 acetyl-CoA-benzylalcohol acetyltransferase
EC 2.3.1.225 protein S-acyltransferase
EC 2.3.1.226 carboxymethylproline synthase
EC 2.3.1.227 GDP-perosamine N-acetyltransferase
EC 2.3.1.228 isovaleryl-homoserine lactone synthase
EC 2.3.1.229 4-coumaroyl-homoserine lactone synthase
EC 2.3.1.230 2-heptyl-4(1H)-quinolone synthase
EC 2.3.1.231 tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase
EC 2.3.1.232 methanol O-anthraniloyltransferase
EC 2.3.1.233 1,3,6,8-tetrahydroxynaphthalene synthase
EC 2.3.1.234 N6-L-threonylcarbamoyladenine synthase
EC 2.3.1.235 tetracenomycin F2 synthase
EC 2.3.1.236 5-methylnaphthoic acid synthase
EC 2.3.1.237 neocarzinostatin naphthoate synthase
EC 2.3.1.238 monacolin J acid methylbutanoate transferase
EC 2.3.1.239 10-deoxymethynolide synthase
EC 2.3.1.240 narbonolide synthase
EC 2.3.1.241 Kdo2-lipid IVA lauroyltransferase
EC 2.3.1.242 Kdo2-lipid IVA palmitoleoyltransferase
EC 2.3.1.243 lauroyl-Kdo2-lipid IVA myristoyltransferase
EC 2.3.1.244 2-methylbutanoate polyketide synthase
EC 2.3.1.245 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase
EC 2.3.1.246 3,5-dihydroxyphenylacetyl-CoA synthase
EC 2.3.1.247 3-keto-5-aminohexanoate cleavage enzyme
EC 2.3.1.248 spermidine disinapoyl transferase
EC 2.3.1.249 spermidine dicoumaroyl transferase
EC 2.3.1.250 [Wnt protein] O-palmitoleoyl transferase
EC 2.3.1.251 lipid IVA palmitoyltransferase
EC 2.3.1.252 mycolipanoate synthase
EC 2.3.1.253 phloroglucinol synthase
EC 2.3.1.254 N-terminal methionine Nα-acetyltransferase NatB
EC 2.3.1.255 N-terminal amino-acid Nα-acetyltransferase NatA
EC 2.3.1.256 N-terminal methionine Nα-acetyltransferase NatC
EC 2.3.1.257 N-terminal L-serine Nα-acetyltransferase NatD
EC 2.3.1.258 N-terminal methionine Nα-acetyltransferase NatE
EC 2.3.1.259 N-terminal methionine Nα-acetyltransferase NatF
EC 2.3.1.260 tetracycline polyketide synthase
EC 2.3.1.261 4-hydroxyphenylalkanoate synthase
EC 2.3.1.262 anthraniloyl-CoA anthraniloyltransferase
EC 2.3.1.263 2-amino-4-oxopentanoate thiolase
EC 2.3.1.264 β-lysine N6-acetyltransferase
EC 2.3.1.265 phosphatidylinositol dimannoside acyltransferase
EC 2.3.1.266 [ribosomal protein S18]-alanine N-acetyltransferase
EC 2.3.1.267 [ribosomal protein S5]-alanine N-acetyltransferase
EC 2.3.1.268 ethanol O-acetyltransferase
EC 2.3.1.269 apolipoprotein N-acyltransferase
EC 2.3.1.270 lyso-ornithine lipid O-acyltransferase
EC 2.3.1.271 L-glutamate-5-semialdehyde N-acetyltransferase
EC 2.3.1.272 2-acetylphloroglucinol acetyltransferase
EC 2.3.1.273 diglucosylglycerate octanoyltransferase
EC 2.3.1.274 phosphate acyltransferase
EC 2.3.1.275 acyl phosphate:glycerol-3-phosphate acyltransferase
EC 2.3.1.276 galactosamine-1-phosphate N-acetyltransferase
EC 2.3.1.277 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase
EC 2.3.1.278 mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase
EC 2.3.1.279 long-chain-acyl-CoA—trehalose acyltransferase
EC 2.3.1.280 (aminoalkyl)phosphonate N-acetyltransferase
EC 2.3.1.281 5-hydroxydodecatetraenal polyketide synthase
EC 2.3.1.282 phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
EC 2.3.1.283 2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
EC 2.3.1.284 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
EC 2.3.1.285 (13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase
EC 2.3.1.286 protein acetyllysine N-acetyltransferase
EC 2.3.1.287 phthioceranic/hydroxyphthioceranic acid synthase
EC 2.3.1.288 2-O-sulfo trehalose long-chain-acyltransferase
EC 2.3.1.289 aureothin polyketide synthase system
EC 2.3.1.290 spectinabilin polyketide synthase system
EC 2.3.1.291 sphingoid base N-palmitoyltransferase

Entries

EC 2.3.1.201

Accepted name: UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase

Reaction: acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate = CoA + UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate

For diagram of reaction, click here

Other name(s): WbpD; WlbB

Systematic name: acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate N-acetyltransferase

Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854-11862. [PMID: 19282284]

2. Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446-5455. [PMID: 19348502]

[EC 2.3.1.201 created 2012]

EC 2.3.1.202

Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase

Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine = CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose

Other name(s): PseH

Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase

Comments: Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C-14C. [PMID: 16751642]

[EC 2.3.1.202 created 2012]

EC 2.3.1.203

Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase

Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine = CoA + UDP-N,N'-diacetylbacillosamine

For diagram of reaction click here.

Glossary: UDP-N,N'-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose

Other name(s): PglD

Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase

Comments: The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-aspargine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659-13669. [PMID: 17087520]

2. Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827-1836. [PMID: 18198901]

3. Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine. Biochemistry 50 (2011) 4936-4948. [PMID: 21542610]

[EC 2.3.1.203 created 2012]

EC 2.3.1.204

Accepted name: octanoyl-[GcvH]:protein N-octanoyltransferase

Reaction: [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine

Glossary: GcvH = glycine cleavage system H]

Other name(s): LipL; octanoyl-[GcvH]:E2 amidotransferase; ywfL (gene name)

Systematic name: [glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase

Comments: In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Christensen, Q.H., Martin, N., Mansilla, M.C., de Mendoza, D. and Cronan, J.E. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol. Microbiol. 80 (2011) 350-363. [PMID: 21338421]

2. Martin, N., Christensen, Q.H., Mansilla, M.C., Cronan, J.E. and de Mendoza, D. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol. Microbiol. 80 (2011) 335-349. [PMID: 21338420]

[EC 2.3.1.204 created 2012]

EC 2.3.1.205

Accepted name: fumigaclavine B O-acetyltransferase

Reaction: acetyl-CoA + fumigaclavine B = CoA + fumigaclavine A

For diagram of reaction click here.

Glossary: fumigaclavine B = 6,8β-dimethylergolin-9-ol
fumigaclavine A = 6,8β-dimethylergolin-9β-yl acetate

Other name(s): FgaAT

Systematic name: acetyl-CoA:fumigaclavine B O-acetyltransferase

Comments: The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Liu, X., Wang, L., Steffan, N., Yin, W.B. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: FgaAT catalyses the acetylation of fumigaclavine B. ChemBioChem. 10 (2009) 2325-2328. [PMID: 19672909]

[EC 2.3.1.205 created 2012]

EC 2.3.1.206

Accepted name: 3,5,7-trioxododecanoyl-CoA synthase

Reaction: 3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2

For diagram of reaction click here.

Other name(s): TKS (ambiguous); olivetol synthase (incorrect)

Systematic name: malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA-forming)

Comments: A polyketide synthase catalysing the first committed step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme was previously thought to also function as a cyclase, but the cyclization is now known to be catalysed by EC 4.4.1.26, olivetolic acid cyclase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Taura, F., Tanaka, S., Taguchi, C., Fukamizu, T., Tanaka, H., Shoyama, Y. and Morimoto, S. Characterization of olivetol synthase, a polyketide synthase putatively involved in cannabinoid biosynthetic pathway. FEBS Lett 583 (2009) 2061-2066. [PMID: 19454282]

2. Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811-12816. [PMID: 22802619]

[EC 2.3.1.206 created 2012]

EC 2.3.1.207

Accepted name: β-ketodecanoyl-[acyl-carrier-protein] synthase

Reaction: octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2

Glossary: [acyl-carrier protein] = [acp]

Systematic name: octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)

Comments: This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via β-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for β-oxidation degradation intermediates into de novo fatty acid biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yuan, Y., Leeds, J.A. and Meredith, T.C. Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis. J. Bacteriol. (2012) . [PMID: 22753057]

[EC 2.3.1.207 created 2012]

EC 2.3.1.208

Accepted name: 4-hydroxycoumarin synthase

Reaction: malonyl-CoA + 2-hydroxybenzoyl-CoA = 2 CoA + 4-hydroxycoumarin + CO2

For diagram of reaction click here.

Glossary: 2-hydroxybenzoyl-CoA = salicyloyl-CoA

Other name(s): BIS2; BIS3

Systematic name: malonyl-CoA:2-hydroxybenzoyl-CoA malonyltransferase

Comments: The enzyme, a polyketide synthase, can also accept benzoyl-CoA as substrate, which it condenses with 3 malonyl-CoA molecules to form 3,5-dihydroxybiphenyl (cf. EC 2.3.1.177, biphenyl synthase) [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Liu, B., Raeth, T., Beuerle, T. and Beerhues, L. A novel 4-hydroxycoumarin biosynthetic pathway. Plant Mol. Biol. 72 (2010) 17-25. [PMID: 19757094]

[EC 2.3.1.208 created 2012]

EC 2.3.1.209

Accepted name: dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase

Reaction: acetyl-CoA + dTDP-4-amino-4,6-dideoxy-α-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-α-D-glucose

Other name(s): VioB

Systematic name: acetyl-CoA:dTDP-4-amino-4,6-dideoxy-α-D-glucose N-acetyltransferase

Comments: The non-activated product, 4-acetamido-4,6-dideoxy-α-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.

References:

1. Wang, Y., Xu, Y., Perepelov, A.V., Qi, Y., Knirel, Y.A., Wang, L. and Feng, L. Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7. J. Bacteriol. 189 (2007) 8626-8635. [PMID: 17905981]

[EC 2.3.1.209 created 2012]

EC 2.3.1.210

Accepted name: dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase

Reaction: acetyl-CoA + dTDP-4-amino-4,6-dideoxy-α-D-galactose = CoA + dTDP-4-acetamido-4,6-dideoxy-α-D-galactose

For diagram of reaction click here.

Glossary: dTDP-4-amino-4,6-dideoxy-α-D-galactose = dTDP-α-D-fucosamine

Other name(s): TDP-fucosamine acetyltransferase; WecD; RffC

Systematic name: acetyl-CoA:dTDP-4-amino-4,6-dideoxy-α-D-galactose N-acetyltransferase

Comments: The product, TDP-4-acetamido-4,6-dideoxy-D-galactose, is utilized in the biosynthesis of enterobacterial common antigen (ECA).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hung, M.N., Rangarajan, E., Munger, C., Nadeau, G., Sulea, T. and Matte, A. Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis. J. Bacteriol. 188 (2006) 5606-5617. [PMID: 16855251]

[EC 2.3.1.210 created 2012]

EC 2.3.1.211

Accepted name: bisdemethoxycurcumin synthase

Reaction: 2 4-coumaroyl-CoA + malonyl-CoA + H2O = 3 CoA + bisdemethoxycurcumin + 2 CO2

For diagram of reaction click here.

Glossary: bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one

Other name(s): CUS; curcuminoid synthase (ambiguous)

Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)

Comments: A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoyl-diketide CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme's cavity and is not released to the environment.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Morita, H., Wanibuchi, K., Nii, H., Kato, R., Sugio, S. and Abe, I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc. Natl. Acad. Sci. USA 107 (2010) 19778-19783. [PMID: 21041675]

[EC 2.3.1.211 created 2013]

EC 2.3.1.212

Accepted name: benzalacetone synthase

Reaction: 4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2

For diagram of reaction click here.

Glossary: 4-hydroxybenzalacetone = 4-(4-hydroxyphenyl)but-3-en-2-one

Other name(s): BAS

Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (4-hydroxybenzalacetone-forming)

Comments: A polyketide synthase that catalyses the C6-C4 skeleton of phenylbutanoids in higher plants.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Borejsza-Wysocki, W. and Hrazdina, G. Aromatic polyketide synthases (purification, characterization, and antibody development to benzalacetone synthase from raspberry fruits). Plant Physiol. 110 (1996) 791-799. [PMID: 12226219]

2. Abe, I., Takahashi, Y., Morita, H. and Noguchi, H. Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum. Eur. J. Biochem. 268 (2001) 3354-3359. [PMID: 11389739]

3. Zheng, D. and Hrazdina, G. Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.). Arch. Biochem. Biophys. 470 (2008) 139-145. [PMID: 18068110]

4. Morita, H., Shimokawa, Y., Tanio, M., Kato, R., Noguchi, H., Sugio, S., Kohno, T. and Abe, I. A structure-based mechanism for benzalacetone synthase from Rheum palmatum. Proc. Natl. Acad. Sci. USA 107 (2010) 669-673. [PMID: 20080733]

[EC 2.3.1.212 created 2013]

EC 2.3.1.213

Accepted name: cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6'''-O-hydroxycinnamoyltransferase

Reaction: 1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside]

For diagram of reaction click here.

Glossary: 1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3',4',5,7-pentahydroxyflavylium

Other name(s): 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6'''-O-(4-hydroxycinnamoyl)transferase

Systematic name: 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6'''-O-(4-hydroxycinnamoyl)transferase

Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582-585.

[EC 2.3.1.213 created 2013]

EC 2.3.1.214

Accepted name: pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4'''-malonyltransferase

Reaction: malonyl-CoA + 4'''-demalonylsalvianin = CoA + salvianin

For diagram of reaction click here.

Glossary: salvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(4,6-di-O-malonyl-β-D-glucoside)
4'''-demalonylsalvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(6-O-malonyl-β-D-glucoside)

Other name(s): malonyl-CoA:anthocyanin 5-glucoside 4'''-O-malonyltransferase; Ss5MaT2

Systematic name: malonyl-CoA:4'''-demalonylsalvianin 4'''-O-malonyltransferase

Comments: Isolated from the plant Salvia splendens (scarlet sage).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Suzuki, H., Sawada, S., Watanabe, K., Nagae, S., Yamaguchi, M.A., Nakayama, T. and Nishino, T. Identification and characterization of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers: an enzyme that is phylogenetically separated from other anthocyanin acyltransferases. Plant J. 38 (2004) 994-1003. [PMID: 15165190]

[EC 2.3.1.214 created 2013]

EC 2.3.1.215

Accepted name: anthocyanidin 3-O-glucoside 6''-O-acyltransferase

Reaction: 4-hydroxycinnamoyl-CoA + an anthocyanidin 3-O-β-D-glucoside = CoA + an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-β-D-glucoside]

For diagram of reaction click here.

Glossary: 4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA
3,4-dihydroxycinnamoyl-CoA = caffeoyl-CoA
cyanidin = 3,3',4',5,7-pentahydroxyflavylium
delphinidin = 3,3',4',5,5',7-hexahydroxyflavylium

Systematic name: 4-hydroxycinnamoyl-CoA:anthocyanin-3-O-glucoside 6''-O-acyltransferase

Comments: Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian). Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. It did not act on delphinidin 3,3',7-tri-O-glucoside. Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Fujiwara, H., Tanaka, Y., Fukui, Y., Ashikari, T., Yamaguchi, M. and Kusumi, T. Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens. Plant Sci. 137 (1998) 87-94.

2. Yonekura-Sakakibara, K., Tanaka, Y., Fukuchi-Mizutani, M., Fujiwara, H., Fukui, Y., Ashikari, T., Murakami, Y., Yamaguchi, M. and Kusumi, T. Molecular and biochemical characterization of a novel hydroxycinnamoyl-CoA: anthocyanin 3-O-glucoside-6"-O-acyltransferase from Perilla frutescens. Plant Cell Physiol 41 (2000) 495-502. [PMID: 10845463]

[EC 2.3.1.215 created 2013]

EC 2.3.1.216

Accepted name: 5,7-dihydroxy-2-methylchromone synthase

Reaction: 5 malonyl-CoA = 5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O

For diagram of reaction click here.

Other name(s): pentaketide chromone synthase

Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (5,7-dihydroxy-2-methyl-4H-chromen-4-one-forming)

Comments: A polyketide synthase from the plant Aloe arborescens (aloe).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Abe, I., Utsumi, Y., Oguro, S., Morita, H., Sano, Y. and Noguchi, H. A plant type III polyketide synthase that produces pentaketide chromone. J. Am. Chem. Soc. 127 (2005) 1362-1363. [PMID: 15686354]

[EC 2.3.1.216 created 2013]

EC 2.3.1.217

Accepted name: curcumin synthase

Reaction: feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2

For diagram of reaction click here.

Glossary: curcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA

Other name(s): CURS; CURS1 (gene name); CURS2 (gene name); CURS3 (gene name)

Systematic name: feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)

Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160-11170. [PMID: 19258320]

2. Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett 583 (2009) 2799-2803. [PMID: 19622354]

3. Katsuyama, Y., Miyazono, K., Tanokura, M., Ohnishi, Y. and Horinouchi, S. Structural and biochemical elucidation of mechanism for decarboxylative condensation of β-keto acid by curcumin synthase. J. Biol. Chem. 286 (2011) 6659-6668. [PMID: 21148316]

[EC 2.3.1.217 created 2013]

EC 2.3.1.218

Accepted name: phenylpropanoylacetyl-CoA synthase

Reaction: (1) feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO2 + CoA
(2) 4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA

For diagram of reaction click here.

Glossary: feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
phenylpropanoylacetyl-CoA = phenylpropanoyl-diketide-CoA

Other name(s): phenylpropanoyl-diketide-CoA synthase; DCS

Systematic name: phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)

Comments: The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160-11170. [PMID: 19258320]

[EC 2.3.1.218 created 2013]

EC 2.3.1.219

Accepted name: demethoxycurcumin synthase

Reaction: (1) 4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
(2) 4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2

For diagram of reaction click here.

Glossary: demethoxycurcumin = (1E,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA

Other name(s): CURS3

Systematic name: 4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-forming)

Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett 583 (2009) 2799-2803. [PMID: 19622354]

[EC 2.3.1.219 created 2013]

EC 2.3.1.220

Accepted name: 2,4,6-trihydroxybenzophenone synthase

Reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2

For diagram of reaction click here.

Other name(s): benzophenone synthase (ambiguous); BPS (ambiguous)

Systematic name: malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)

Comments: Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3',4,6-tetrahydroxybenzophenone synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schmidt, W. and Beerhues, L. Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum L. FEBS Lett 420 (1997) 143-146. [PMID: 9459298]

2. Nualkaew, N., Morita, H., Shimokawa, Y., Kinjo, K., Kushiro, T., De-Eknamkul, W., Ebizuka, Y. and Abe, I. Benzophenone synthase from Garcinia mangostana L. pericarps. Phytochemistry 77 (2012) 60-69. [PMID: 22390826]

[EC 2.3.1.220 created 2013]

EC 2.3.1.221

Accepted name: noranthrone synthase

Reaction: 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O

For diagram of reaction click here.

Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one

Other name(s): polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase

Systematic name: malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)

Comments: A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243-246. [PMID: 18403714]

2. Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139-1143. [PMID: 19847268]

3. Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246-6251. [PMID: 20332208]

[EC 2.3.1.221 created 2013]

EC 2.3.1.222

Accepted name: phosphate propanoyltransferase

Reaction: propanoyl-CoA + phosphate = CoA + propanoyl phosphate

Other name(s): PduL

Systematic name: propanoyl-CoA:phosphate propanoyltransferase

Comments: Part of the degradation pathway for propane-1,2-diol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Liu, Y., Leal, N.A., Sampson, E.M., Johnson, C.L., Havemann, G.D. and Bobik, T.A. PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 189 (2007) 1589-1596. [PMID: 17158662]

[EC 2.3.1.222 created 2013]

EC 2.3.1.223

Accepted name: 3-oxo-5,6-didehydrosuberyl-CoA thiolase

Reaction: 2,3-didehydroadipoyl-CoA + acetyl-CoA = CoA + 3-oxo-5,6-didehydrosuberoyl-CoA

Glossary: 2,3-didehydroadipoyl-CoA = 5-carboxypent-2-enoyl-CoA
3-oxo-5,6-didehydrosuberoyl-CoA = 7-carboxy-3-oxohept-5-enoyl-CoA

Other name(s): paaJ (gene name)

Systematic name: 2,3-didehydroadipoyl-CoA:acetyl-CoA C-didehydroadipoyltransferase (double bond migration)

Comments: The enzyme acts in the opposite direction. The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174 (3-oxoadipyl-CoA thiolase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Teufel, R., Mascaraque, V., Ismail, W., Voss, M., Perera, J., Eisenreich, W., Haehnel, W. and Fuchs, G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. USA 107 (2010) 14390-14395. [PMID: 20660314]

[EC 2.3.1.223 created 2013]

EC 2.3.1.224

Accepted name: acetyl-CoA-benzylalcohol acetyltransferase

Reaction: (1) acetyl-CoA + benzyl alcohol = CoA + benzyl acetate
(2) acetyl-CoA + cinnamyl alcohol = CoA + cinnamyl acetate

Other name(s): BEAT

Systematic name: acetyl-CoA:benzylalcohol O-acetyltransferase

Comments: The enzyme is found in flowers like Clarkia breweri, where it is important for floral scent production. Unlike EC 2.3.1.84, alcohol O-acetyltransferase, this enzyme is active with alcohols that contain a benzyl ring.

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Dudareva, N., D'Auria, J.C., Nam, K.H., Raguso, R.A. and Pichersky, E. Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J. 14 (1998) 297-304. [PMID: 9628024]

[EC 2.3.1.224 created 2013]

EC 2.3.1.225

Accepted name: protein S-acyltransferase

Reaction: palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA

Other name(s): DHHC palmitoyl transferase; S-protein acyltransferase; G-protein palmitoyltransferase

Systematic name: palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase

Comments: The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Dunphy, J.T., Greentree, W.K., Manahan, C.L. and Linder, M.E. G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271 (1996) 7154-7159. [PMID: 8636152]

2. Veit, M., Dietrich, L.E. and Ungermann, C. Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS Lett 540 (2003) 101-105. [PMID: 12681491]

3. Batistic, O. Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family. Plant Physiol. 160 (2012) 1597-1612. [PMID: 22968831]

4. Jennings, B.C. and Linder, M.E. DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. J. Biol. Chem. 287 (2012) 7236-7245. [PMID: 22247542]

5. Zhou, L.Z., Li, S., Feng, Q.N., Zhang, Y.L., Zhao, X., Zeng, Y.L., Wang, H., Jiang, L. and Zhang, Y. Protein S-acyl transferase10 is critical for development and salt tolerance in Arabidopsis. Plant Cell 25 (2013) 1093-1107. [PMID: 23482856]

[EC 2.3.1.225 created 2013]

EC 2.3.1.226

Accepted name: carboxymethylproline synthase

Reaction: malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2

Other name(s): CarB (ambiguous)

Systematic name: malonyl-CoA:(S)-1-pyrroline-5-carboxylate malonyltransferase (cyclizing)

Comments: The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Sleeman, M.C. and Schofield, C.J. Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. J. Biol. Chem. 279 (2004) 6730-6736. [PMID: 14625287]

2. Gerratana, B., Arnett, S.O., Stapon, A. and Townsend, C.A. Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily. Biochemistry 43 (2004) 15936-15945. [PMID: 15595850]

3. Sorensen, J.L., Sleeman, M.C. and Schofield, C.J. Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB)—implications for carbapenem biosynthesis. Chem. Commun. (Camb.) (2005) 1155-1157. [PMID: 15726176]

4. Sleeman, M.C., Sorensen, J.L., Batchelar, E.T., McDonough, M.A. and Schofield, C.J. Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis. J. Biol. Chem. 280 (2005) 34956-34965. [PMID: 16096274]

5. Batchelar, E.T., Hamed, R.B., Ducho, C., Claridge, T.D., Edelmann, M.J., Kessler, B. and Schofield, C.J. Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily. Angew. Chem. Int. Ed. Engl. 47 (2008) 9322-9325. [PMID: 18972478]

6. Hamed, R.B., Gomez-Castellanos, J.R., Thalhammer, A., Harding, D., Ducho, C., Claridge, T.D. and Schofield, C.J. Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases. Nat. Chem. 3 (2011) 365-371. [PMID: 21505494]

[EC 2.3.1.226 created 2013]

EC 2.3.1.227

Accepted name: GDP-perosamine N-acetyltransferase

Reaction: acetyl-CoA + GDP-4-amino-4,6-dideoxy-α-D-mannose = CoA + GDP-4-acetamido-4,6-dideoxy-α-D-mannose

Glossary: GDP-4-amino-4,6-dideoxy-α-D-mannose = GDP-α-D-perosamine
GDP-4-acetamido-4,6-dideoxy-α-D-mannose = GDP-N-acetyl-α-D-perosamine

Other name(s): perB (gene name); GDP-α-D-perosamine N-acetyltransferase

Systematic name: acetyl-CoA:GDP-4-amino-4,6-dideoxy-α-D-mannose N-acetyltransferase

Comments: D-Perosamine is one of several dideoxy sugars found in the O-antigen component of the outer membrane lipopolysaccharides of Gram-negative bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Albermann, C. and Beuttler, H. Identification of the GDP-N-acetyl-D-perosamine producing enzymes from Escherichia coli O157:H7. FEBS Lett 582 (2008) 479-484. [PMID: 18201574]

[EC 2.3.1.227 created 2013]

EC 2.3.1.228

Accepted name: isovaleryl-homoserine lactone synthase

Reaction: isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5'-thioadenosine + N-isovaleryl-L-homoserine lactone

Other name(s): IV-HSL synthase; BjaI

Systematic name: isovaleryl-CoA:S-adenosyl-L-methionine isovaleryltranserase (lactone-forming, methylthioadenosine-releasing)

Comments: The enzyme, found in the bacterium Bradyrhizobium japonicum, does not accept isovaleryl-[acyl-carrier protein] as acyl donor (cf. EC 2.3.1.184, acyl-homoserine-lactone synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lindemann, A., Pessi, G., Schaefer, A.L., Mattmann, M.E., Christensen, Q.H., Kessler, A., Hennecke, H., Blackwell, H.E., Greenberg, E.P. and Harwood, C.S. Isovaleryl-homoserine lactone, an unusual branched-chain quorum-sensing signal from the soybean symbiont Bradyrhizobium japonicum. Proc. Natl. Acad. Sci. USA 108 (2011) 16765-16770. [PMID: 21949379]

[EC 2.3.1.228 created 2013]

EC 2.3.1.229

Accepted name: 4-coumaroyl-homoserine lactone synthase

Reaction: 4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone

Other name(s): p-coumaryl-homoserine lactone synthase; RpaI

Systematic name: 4-coumaroyl-CoA:S-adenosyl-L-methionine trans-4-coumaroyltranserase (lactone-forming, methylthioadenosine-releasing)

Comments: The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schaefer, A.L., Greenberg, E.P., Oliver, C.M., Oda, Y., Huang, J.J., Bittan-Banin, G., Peres, C.M., Schmidt, S., Juhaszova, K., Sufrin, J.R. and Harwood, C.S. A new class of homoserine lactone quorum-sensing signals. Nature 454 (2008) 595-599. [PMID: 18563084]

[EC 2.3.1.229 created 2013]

EC 2.3.1.230

Accepted name: 2-heptyl-4(1H)-quinolone synthase

Reaction: octanoyl-CoA + 2-aminobenzoylacetate = 2-heptyl-4(1H)-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + 2-aminobenzoylacetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4(1H)-quinolone + H2O

Glossary: 4-hydroxy-2(1H)-quinolone = 2,4-dihydroxyquinoline
2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
anthraniloyl-CoA = 2-aminobenzoyl-CoA

Other name(s): pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)

Systematic name: octanoyl-CoA:2-aminobenzoylacetate octanoyltransferase

Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with 2-aminobenzoylacetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481-1491. [PMID: 24239007]

2. Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone Signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610-6624. [PMID: 26811339]

[EC 2.3.1.230 created 2013, modified 2017]

EC 2.3.1.231

Accepted name: tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase

Reaction: S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe + CO2 = S-adenosyl-L-homocysteine + wybutosine37 in tRNAPhe

For diagram of reaction, click here

Glossary: wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-{(3S)-3-(methoxycarbonyl)-3-(methoxycarbonylamino)propyl}-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one

Other name(s): TYW4 (ambiguous); tRNA-yW synthesizing enzyme-4 (ambiguous)

Systematic name: S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)

Comments: The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-[2-hydroxy-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.1.1.290, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Noma, A., Kirino, Y., Ikeuchi, Y. and Suzuki, T. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25 (2006) 2142-2154. [PMID: 16642040]

2. Suzuki, Y., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4. Nucleic Acids Res. 37 (2009) 2910-2925. [PMID: 19287006]

3. Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and Nureki, O. Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification. Nucleic Acids Res. 39 (2011) 1576-1585. [PMID: 20972222]

[EC 2.3.1.231 created 2013]

EC 2.3.1.232

Accepted name: methanol O-anthraniloyltransferase

Reaction: anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate

Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA

Other name(s): AMAT; anthraniloyl-coenzyme A (CoA):methanol acyltransferase

Systematic name: anthraniloyl-coenzyme A:methanol O-anthraniloyltransferase

Comments: The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wang, J. and De Luca, V. The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate. Plant J. 44 (2005) 606-619. [PMID: 16262710]

[EC 2.3.1.232 created 2014]

EC 2.3.1.233

Accepted name: 1,3,6,8-tetrahydroxynaphthalene synthase

Reaction: 5 malonyl-CoA = 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O

For diagram of reaction click here.

Other name(s): PKS1; THNS; SCO1206; RppA

Systematic name: malonyl-CoA C-acyl transferase (1,3,6,8-tetrahydroxynaphthalene forming)

Comments: Isolated from the fungus Colletotrichum lagenarium [1], and the bacteria Streptomyces coelicolor [2,3] and Streptomyces peucetius [4]. It only uses malonyl-CoA, without invovement of acetyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Fujii, I., Mori, Y., Watanabe, A., Kubo, Y., Tsuji, G. and Ebizuka, Y. Enzymatic synthesis of 1,3,6,8-tetrahydroxynaphthalene solely from malonyl coenzyme A by a fungal iterative type I polyketide synthase PKS1. Biochemistry 39 (2000) 8853-8858. [PMID: 10913297]

2. Izumikawa, M., Shipley, P.R., Hopke, J.N., O'Hare, T., Xiang, L., Noel, J.P. and Moore, B.S. Expression and characterization of the type III polyketide synthase 1,3,6,8-tetrahydroxynaphthalene synthase from Streptomyces coelicolor A3(2). J Ind Microbiol Biotechnol 30 (2003) 510-515. [PMID: 12905073]

3. Austin, M.B., Izumikawa, M., Bowman, M.E., Udwary, D.W., Ferrer, J.L., Moore, B.S. and Noel, J.P. Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates. J. Biol. Chem. 279 (2004) 45162-45174. [PMID: 15265863]

4. Ghimire, G.P., Oh, T.J., Liou, K. and Sohng, J.K. Identification of a cryptic type III polyketide synthase (1,3,6,8-tetrahydroxynaphthalene synthase) from Streptomyces peucetius ATCC 27952. Mol. Cells 26 (2008) 362-367. [PMID: 18612244]

[EC 2.3.1.233 created 2014]

EC 2.3.1.234

Accepted name: N6-L-threonylcarbamoyladenine synthase

Reaction: L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N6-L-threonylcarbamoyladenine37 in tRNA

For diagram of reaction click here.

Glossary: N6-L-threonylcarbamoyladenine37 = t6A37

Other name(s): t6A synthase; Kae1; ygjD (gene name); Qri7

Systematic name: L-threonylcarbamoyladenylate:adenine37 in tRNA N6-L-threonylcarbamoyltransferase

Comments: The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg [3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Lauhon, C.T. Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Biochemistry 51 (2012) 8950-8963. [PMID: 23072323]

2. Deutsch, C., El Yacoubi, B., de Crecy-Lagard, V. and Iwata-Reuyl, D. Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. J. Biol. Chem. 287 (2012) 13666-13673. [PMID: 22378793]

3. Perrochia, L., Crozat, E., Hecker, A., Zhang, W., Bareille, J., Collinet, B., van Tilbeurgh, H., Forterre, P. and Basta, T. In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya. Nucleic Acids Res. 41 (2013) 1953-1964. [PMID: 23258706]

4. Wan, L.C.K., Mao, D.Y.L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R.K., Lissina, E., Nislow, C., Caudy, A.A., Durocher, D. and Sicheri, F. Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41 (2013) 6332-6346. [PMID: 23620299]

[EC 2.3.1.234 created 2014 as EC 2.6.99.4, transferred 2014 to EC 2.3.1.234]

EC 2.3.1.235

Accepted name: tetracenomycin F2 synthase

Reaction: 10 malonyl-CoA = tetracenomycin F2 + 10 CoA + 10 CO2 + 2 H2O

For diagram of reaction click here.

Glossary: tetracenomycin F2 = 4-(3-acetyl-4,5,7,10-tetrahydroxyanthracen-2-yl)-3-oxobutanoic acid

Other name(s): TCM PKS

Systematic name: malonyl-CoA:acetate malonyltransferase (tetracenomycin F2 forming)

Comments: A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens. It involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN). A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit. Additional two-carbon units are added from nine more malonyl-CoA molecules.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bao, W., Wendt-Pienkowski, E. and Hutchinson, C.R. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37 (1998) 8132-8138. [PMID: 9609708]

[EC 2.3.1.235 created 2014]

EC 2.3.1.236

Accepted name: 5-methylnaphthoic acid synthase

Reaction: acetyl-CoA + 5 malonyl-CoA + 3 NADPH + 3 H+ = 5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 4 H2O + 3 NADP+

For diagram of reaction click here.

Other name(s): AziB

Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (5-methyl-1-naphthoic acid forming)

Comments: A multi-domain polyketide synthase involved in the synthesis of azinomycin B in the bacterium Streptomyces griseofuscus.

References:

1. Zhao, Q., He, Q., Ding, W., Tang, M., Kang, Q., Yu, Y., Deng, W., Zhang, Q., Fang, J., Tang, G. and Liu, W. Characterization of the azinomycin B biosynthetic gene cluster revealing a different iterative type I polyketide synthase for naphthoate biosynthesis. Chem. Biol. 15 (2008) 693-705. [PMID: 18635006]

[EC 2.3.1.236 created 2014]

EC 2.3.1.237

Accepted name: neocarzinostatin naphthoate synthase

Reaction: acetyl-CoA + 5 malonyl-CoA + 2 NADPH + 2 H+ = 2-hydroxy-5-methyl-1-naphthoate + 6 CoA + 5 CO2 + 3 H2O + 2 NADP+

For diagram of reaction click here.

Other name(s): naphthoic acid synthase; NNS; ncsB (gene name)

Systematic name: malonyl-CoA:acetyl-CoA malonyltransferase (2-hydroxy-5-methyl-1-naphthoic acid forming)

Comments: A multi-domain polyketide synthase involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sthapit, B., Oh, T.J., Lamichhane, R., Liou, K., Lee, H.C., Kim, C.G. and Sohng, J.K. Neocarzinostatin naphthoate synthase: an unique iterative type I PKS from neocarzinostatin producer Streptomyces carzinostaticus. FEBS Lett 566 (2004) 201-206. [PMID: 15147895]

[EC 2.3.1.237 created 2014]

EC 2.3.1.238

Accepted name: monacolin J acid methylbutanoate transferase

Reaction: monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase]

For diagram of reaction click here.

Glossary: monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
lovastatin acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-2,6-dimethyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate

Other name(s): LovD

Systematic name: monacolin J acid:(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] (S)-2-methylbutanoate transferase

Comments: The enzyme catalyses the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368-1372. [PMID: 10334994]

2. Xie, X., Watanabe, K., Wojcicki, W.A., Wang, C.C. and Tang, Y. Biosynthesis of lovastatin analogs with a broadly specific acyltransferase. Chem. Biol. 13 (2006) 1161-1169. [PMID: 17113998]

3. Xie, X., Meehan, M.J., Xu, W., Dorrestein, P.C. and Tang, Y. Acyltransferase mediated polyketide release from a fungal megasynthase. J. Am. Chem. Soc. 131 (2009) 8388-8389. [PMID: 19530726]

[EC 2.3.1.238 created 2014]

EC 2.3.1.239

Accepted name: 10-deoxymethynolide synthase

Reaction: malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O

For diagram of reaction click here.

Other name(s): pikromycin PKS

Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming)

Comments: The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae. The enzyme also produces narbonolide (see EC 2.3.1.240, narbonolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590-12597. [PMID: 12379101]

2. Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944-954. [PMID: 17719493]

3. Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537-1543. [PMID: 19437523]

4. Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560-564. [PMID: 24965656]

[EC 2.3.1.239 created 2014]

EC 2.3.1.240

Accepted name: narbonolide synthase

Reaction: malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O

For diagram of reaction click here.

Other name(s): pikromycin PKS

Systematic name: (2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (narbonolide forming)

Comments: The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239, 10-deoxymethynolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Lu, H., Tsai, S.C., Khosla, C. and Cane, D.E. Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase. Biochemistry 41 (2002) 12590-12597. [PMID: 12379101]

2. Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W. and Sherman, D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944-954. [PMID: 17719493]

3. Yan, J., Gupta, S., Sherman, D.H. and Reynolds, K.A. Functional dissection of a multimodular polypeptide of the pikromycin polyketide synthase into monomodules by using a matched pair of heterologous docking domains. Chembiochem 10 (2009) 1537-1543. [PMID: 19437523]

4. Whicher, J.R., Dutta, S., Hansen, D.A., Hale, W.A., Chemler, J.A., Dosey, A.M., Narayan, A.R., Hakansson, K., Sherman, D.H., Smith, J.L. and Skiniotis, G. Structural rearrangements of a polyketide synthase module during its catalytic cycle. Nature 510 (2014) 560-564. [PMID: 24965656]

[EC 2.3.1.240 created 2014]

EC 2.3.1.241

Accepted name: Kdo2-lipid IVA lauroyltransferase

Reaction: a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA = dodecanoyl-Kdo2-lipid IVA + an [acyl-carrier protein]

For diagram of reaction click here.

Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA
dodecanoyl = lauroyl
dodecanoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s): LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase; (Kdo)2-lipid IVA lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase

Systematic name: dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095-12102. [PMID: 8662613]

2. Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623-8637. [PMID: 18656959]

[EC 2.3.1.241 created 2014]

EC 2.3.1.242

Accepted name: Kdo2-lipid IVA palmitoleoyltransferase

Reaction: a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo2-lipid IVA = (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA + an [acyl-carrier protein]

For diagram of reaction click here.

Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA
(9Z)-hexadec-9-enoyl = palmitoleoyl
(9Z)-hexadec-9-enoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-{(3R)-3-[(9Z)-hexadec-9-enoyloxy]tetradecanamido}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s): LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase; (Kdo)2-lipid IVA palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA palmitoleoyltransferase

Systematic name: (9Z)-hexadec-9-enoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-palmitoleoyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Carty, S.M., Sreekumar, K.R. and Raetz, C.R. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274 (1999) 9677-9685. [PMID: 10092655]

2. Vorachek-Warren, M.K., Carty, S.M., Lin, S., Cotter, R.J. and Raetz, C.R. An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C. J. Biol. Chem. 277 (2002) 14186-14193. [PMID: 11830594]

[EC 2.3.1.242 created 2014]

EC 2.3.1.243

Accepted name: lauroyl-Kdo2-lipid IVA myristoyltransferase

Reaction: a tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA = dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA + an [acyl-carrier protein]

For diagram of reaction click here.

Glossary: Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA
dodecanoyl = lauroyl
tetradecanoyl = myristoyl
dodecanoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s): MsbB acyltransferase; lpxM (gene name); myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase

Systematic name: tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353-10360. [PMID: 9099672]

[EC 2.3.1.243 created 2014]

EC 2.3.1.244

Accepted name: 2-methylbutanoate polyketide synthase

Reaction: acetyl-CoA + malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + 2 H+ + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + CO2 + 2 NADP+ + S-adenosyl-L-homocysteine + H2O

For diagram of reaction click here.

Other name(s): LovF

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (2-methylbutanoate-forming)

Comments: This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus. The overall reaction comprises a single condensation reaction followed by α-methylation, β-ketoreduction, dehydration, and α,β enoyl reduction.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368-1372. [PMID: 10334994]

2. Meehan, M.J., Xie, X., Zhao, X., Xu, W., Tang, Y. and Dorrestein, P.C. FT-ICR-MS characterization of intermediates in the biosynthesis of the α-methylbutyrate side chain of lovastatin by the 277 kDa polyketide synthase LovF. Biochemistry 50 (2011) 287-299. [PMID: 21069965]

[EC 2.3.1.244 created 2015]

EC 2.3.1.245

Accepted name: 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase

Reaction: glycerone phosphate + acetyl-CoA = 3-hydroxy-5-phosphooxypentane-2,4-dione + CoA

Glossary: (4S)-4,5-dihydroxypentane-2,3-dione = autoinducer 2 = AI-2

Other name(s): lsrF (gene name); 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase

Systematic name: acetyl-CoA:glycerone phosphate C-acetyltransferase

Comments: The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Diaz, Z., Xavier, K.B. and Miller, S.T. The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF. PLoS One 4 (2009) e6820. [PMID: 19714241]

2. Marques, J.C., Oh, I.K., Ly, D.C., Lamosa, P., Ventura, M.R., Miller, S.T. and Xavier, K.B. LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2. Proc. Natl. Acad. Sci. USA 111 (2014) 14235-14240. [PMID: 25225400]

[EC 2.3.1.245 created 2015]

EC 2.3.1.246

Accepted name: 3,5-dihydroxyphenylacetyl-CoA synthase

Reaction: 4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O

Other name(s): DpgA

Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (3,5-dihydroxyphenylacetyl-CoA-forming)

Comments: The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Pfeifer, V., Nicholson, G.J., Ries, J., Recktenwald, J., Schefer, A.B., Shawky, R.M., Schroder, J., Wohlleben, W. and Pelzer, S. A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine. J. Biol. Chem. 276 (2001) 38370-38377. [PMID: 11495926]

2. Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901-14906. [PMID: 11752437]

3. Tseng, C.C., McLoughlin, S.M., Kelleher, N.L. and Walsh, C.T. Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase. Biochemistry 43 (2004) 970-980. [PMID: 14744141]

4. Wu, H.C., Li, Y.S., Liu, Y.C., Lyu, S.Y., Wu, C.J. and Li, T.L. Chain elongation and cyclization in type III PKS DpgA. Chembiochem 13 (2012) 862-871. [PMID: 22492619]

[EC 2.3.1.246 created 2015]

EC 2.3.1.247

Accepted name: 3-keto-5-aminohexanoate cleavage enzyme

Reaction: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = L-3-aminobutanoyl-CoA + acetoacetate

For diagram of reaction click here.

Glossary: L-3-aminobutyryl-CoA = (3S)-3-aminobutanoyl-CoA

Other name(s): kce (gene name)

Systematic name: (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase

Comments: Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Barker, H.A., Kahn, J.M. and Hedrick, L. Pathway of lysine degradation in Fusobacterium nucleatum. J. Bacteriol. 152 (1982) 201-207. [PMID: 6811551]

2. Kreimeyer, A., Perret, A., Lechaplais, C., Vallenet, D., Medigue, C., Salanoubat, M. and Weissenbach, J. Identification of the last unknown genes in the fermentation pathway of lysine. J. Biol. Chem. 282 (2007) 7191-7197. [PMID: 17166837]

3. Bellinzoni, M., Bastard, K., Perret, A., Zaparucha, A., Perchat, N., Vergne, C., Wagner, T., de Melo-Minardi, R.C., Artiguenave, F., Cohen, G.N., Weissenbach, J., Salanoubat, M. and Alzari, P.M. 3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation. J. Biol. Chem. 286 (2011) 27399-27405. [PMID: 21632536]

[EC 2.3.1.247 created 2015]

EC 2.3.1.248

Accepted name: spermidine disinapoyl transferase

Reaction: 2 sinapoyl-CoA + spermidine = 2 CoA + N1,N8-bis(sinapoyl)-spermidine

Other name(s): SDT

Systematic name: sinapoyl-CoA:spermidine N-(hydroxycinnamoyl)transferase

Comments: The enzyme from the plant Arabidopsis thaliana has no activity with 4-coumaroyl-CoA (cf. EC 2.3.1.249, spermidine dicoumaroyl transferase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318-333. [PMID: 19168716]

[EC 2.3.1.248 created 2015]

EC 2.3.1.249

Accepted name: spermidine dicoumaroyl transferase

Reaction: 2 4-coumaroyl-CoA + spermidine = 2 CoA + N1,N8-bis(4-coumaroyl)-spermidine

Other name(s): SCT

Systematic name: 4-coumaroyl-CoA:spermidine N-(hydroxycinnamoyl)transferase

Comments: The enzyme from the plant Arabidopsis thaliana has no activity with sinapoyl-CoA (cf. EC 2.3.1.248, spermidine disinapoyl transferase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Luo, J., Fuell, C., Parr, A., Hill, L., Bailey, P., Elliott, K., Fairhurst, S.A., Martin, C. and Michael, A.J. A novel polyamine acyltransferase responsible for the accumulation of spermidine conjugates in Arabidopsis seed. Plant Cell 21 (2009) 318-333. [PMID: 19168716]

[EC 2.3.1.249 created 2015]

EC 2.3.1.250

Accepted name: [Wnt protein] O-palmitoleoyl transferase

Reaction: (9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine

Glossary: (9Z)-hexadec-9-enoate = palmitoleoate

Other name(s): porcupine; PORCN (gene name)

Systematic name: (9Z)-hexadec-9-enoyl-CoA:[Wnt]-L-serine O-hexadecenoyltransferase

Comments: The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser209 in human Wnt3a and Ser224 in chicken WNT1 [2,3]. The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo [1]. cf. EC 3.1.1.98, [Wnt protein]-O-palmitoleoyl-L-serine hydrolase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Takada, R., Satomi, Y., Kurata, T., Ueno, N., Norioka, S., Kondoh, H., Takao, T. and Takada, S. Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion. Dev Cell 11 (2006) 791-801. [PMID: 17141155]

2. Gao, X. and Hannoush, R.N. Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nat. Chem. Biol. 10 (2014) 61-68. [PMID: 24292069]

3. Miranda, M., Galli, L.M., Enriquez, M., Szabo, L.A., Gao, X., Hannoush, R.N. and Burrus, L.W. Identification of the WNT1 residues required for palmitoylation by Porcupine. FEBS Lett. 588 (2014) 4815-4824. [PMID: 25451226]

[EC 2.3.1.250 created 2015]

EC 2.3.1.251

Accepted name: lipid IVA palmitoyltransferase

Reaction: (1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
(2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB
(3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB

For diagram of reaction click here.

Glossary: palmitoyl = hexadecanoyl
hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IIB = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IVB = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate

Other name(s): PagP; crcA (gene name)

Systematic name: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase

Comments: Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IVA.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I. and Raetz, C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19 (2000) 5071-5080. [PMID: 11013210]

2. Cuesta-Seijo, J.A., Neale, C., Khan, M.A., Moktar, J., Tran, C.D., Bishop, R.E., Pomes, R. and Prive, G.G. PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 (2010) 1210-1219. [PMID: 20826347]

[EC 2.3.1.251 created 2015]

EC 2.3.1.252

Accepted name: mycolipanoate synthase

Reaction: a long-chain acyl-CoA + 3 (R)-methylmalonyl-CoA + 6 NADPH + 6 H+ + holo-[mycolipanoate synthase] = mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO2 + 6 NADP+ + 3 H2O

Glossary: mycolipanoic acid = (2S,4S,6S)-2,4,6-trimethyl-very-long-chain fatty acid

Other name(s): msl3 (gene name); Pks3/4; mycolipanoic acid synthase

Systematic name: long-chain acyl-CoA:methylmalonyl-CoA C-acyltransferase (mycolipanoate-forming)

Comments: This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyltetracosanoate (C27-mycolipanoate). Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem. 276 (2001) 16833-16839. [PMID: 11278910]

2. Dubey, V.S., Sirakova, T.D. and Kolattukudy, P.E. Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation. Mol. Microbiol. 45 (2002) 1451-1459. [PMID: 12207710]

[EC 2.3.1.252 created 2016]

EC 2.3.1.253

Accepted name: phloroglucinol synthase

Reaction: 3 malonyl-CoA = phloroglucinol + 3 CO2 + 3 CoA

For diagram of reaction click here.

Glossary: phloroglucinol = 1,3,5-trihydroxybenzene

Other name(s): phlD (gene name)

Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (decarboxylating, phloroglucinol-forming)

Comments: The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a type III polyketide synthase. The mechanism involves the cyclization of an activated 3,5-dioxoheptanedioate intermediate. The enzyme exhibits broad substrate specificity, and can accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoA as the starter molecules, forming 6-(polyoxoalkylated)-α-pyrones by sequential condensation with malonyl-CoA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Achkar, J., Xian, M., Zhao, H. and Frost, J.W. Biosynthesis of phloroglucinol. J. Am. Chem. Soc. 127 (2005) 5332-5333.

2. Zha, W., Rubin-Pitel, S.B. and Zhao, H. Characterization of the substrate specificity of PhlD, a type III polyketide synthase from Pseudomonas fluorescens. J. Biol. Chem. 281 (2006) 32036-32047. [PMID: 16931521]

[EC 2.3.1.253 created 2016]

EC 2.3.1.254

Accepted name: N-terminal methionine Nα-acetyltransferase NatB

Reaction: (1) acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutamyl-[protein] + CoA

Other name(s): NAA20 (gene name); NAA25 (gene name)

Systematic name: acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nα-acetyltransferase

Comments: N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Starheim, K.K., Arnesen, T., Gromyko, D., Ryningen, A., Varhaug, J.E. and Lillehaug, J.R. Identification of the human Nα-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression. Biochem. J. 415 (2008) 325-331. [PMID: 18570629]

2. Ferrandez-Ayela, A., Micol-Ponce, R., Sanchez-Garcia, A.B., Alonso-Peral, M.M., Micol, J.L. and Ponce, M.R. Mutation of an Arabidopsis NatB N-α-terminal acetylation complex component causes pleiotropic developmental defects. PLoS One 8 (2013) e80697. [PMID: 24244708]

3. Lee, K.E., Ahn, J.Y., Kim, J.M. and Hwang, C.S. Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae. J Microbiol 52 (2014) 842-848. [PMID: 25163837]

[EC 2.3.1.254 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.254]

EC 2.3.1.255

Accepted name: N-terminal amino-acid Nα-acetyltransferase NatA

Reaction: (1) acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-Nα-acetyl-glycyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-alanyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-seryl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-valyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-Nα-acetyl-L-cysteinyl-[protein] + CoA
(6) acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-threonyl-[protein] + CoA

Other name(s): NAA10 (gene name); NAA15 (gene name); ARD1 (gene name)

Systematic name: acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nα-acetyltransferase

Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mullen, J.R., Kayne, P.S., Moerschell, R.P., Tsunasawa, S., Gribskov, M., Colavito-Shepanski, M., Grunstein, M., Sherman, F. and Sternglanz, R. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J. 8 (1989) 2067-2075. [PMID: 2551674]

2. Park, E.C. and Szostak, J.W. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 11 (1992) 2087-2093. [PMID: 1600941]

3. Sugiura, N., Adams, S.M. and Corriveau, R.A. An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development. J. Biol. Chem. 278 (2003) 40113-40120. [PMID: 12888564]

4. Gautschi, M., Just, S., Mun, A., Ross, S., Rucknagel, P., Dubaquie, Y., Ehrenhofer-Murray, A. and Rospert, S. The yeast Nα-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell Biol. 23 (2003) 7403-7414. [PMID: 14517307]

5. Xu, F., Huang, Y., Li, L., Gannon, P., Linster, E., Huber, M., Kapos, P., Bienvenut, W., Polevoda, B., Meinnel, T., Hell, R., Giglione, C., Zhang, Y., Wirtz, M., Chen, S. and Li, X. Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis. Plant Cell 27 (2015) 1547-1562. [PMID: 25966763]

6. Dorfel, M.J. and Lyon, G.J. The biological functions of Naa10 - From amino-terminal acetylation to human disease. Gene 567 (2015) 103-131. [PMID: 25987439]

[EC 2.3.1.255 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.255]

EC 2.3.1.256

Accepted name: N-terminal methionine Nα-acetyltransferase NatC

Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA

Other name(s): NAA30 (gene name); NAA35 (gene name); NAA38 (gene name); MAK3 (gene name); MAK10 (gene name); MAK31 (gene name)

Systematic name: acetyl-CoA:N-terminal-Met-Leu/Ile/Phe/Trp/Tyr-[protein] Met Nα-acetyltransferase

Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Polevoda, B. and Sherman, F. NatC Nα-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p. J. Biol. Chem. 276 (2001) 20154-20159. [PMID: 11274203]

2. Polevoda, B. and Sherman, F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308 (2003) 1-11. [PMID: 12890471]

3. Pesaresi, P., Gardner, N.A., Masiero, S., Dietzmann, A., Eichacker, L., Wickner, R., Salamini, F. and Leister, D. Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis. Plant Cell 15 (2003) 1817-1832. [PMID: 12897255]

4. Wenzlau, J.M., Garl, P.J., Simpson, P., Stenmark, K.R., West, J., Artinger, K.B., Nemenoff, R.A. and Weiser-Evans, M.C. Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development. Circ. Res. 98 (2006) 846-855. [PMID: 16484612]

5. Starheim, K.K., Gromyko, D., Evjenth, R., Ryningen, A., Varhaug, J.E., Lillehaug, J.R. and Arnesen, T. Knockdown of human Nα-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell Biol. 29 (2009) 3569-3581. [PMID: 19398576]

[EC 2.3.1.256 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.256]

EC 2.3.1.257

Accepted name: N-terminal L-serine Nα-acetyltransferase NatD

Reaction: (1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nα-acetyl-L-seryl-[histone H4] + CoA
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nα-acetyl-L-seryl-[histone H2A] + CoA

Other name(s): NAA40 (gene name)

Systematic name: acetyl-CoA:N-terminal-L-seryl-[histone 4/2A] L-serine Nα-acetyltransferase

Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Song, O.K., Wang, X., Waterborg, J.H. and Sternglanz, R. An Nα-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J. Biol. Chem. 278 (2003) 38109-38112. [PMID: 12915400]

2. Polevoda, B., Hoskins, J. and Sherman, F. Properties of Nat4, an Nα-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4. Mol. Cell Biol. 29 (2009) 2913-2924. [PMID: 19332560]

3. Magin, R.S., Liszczak, G.P. and Marmorstein, R. The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD. Structure 23 (2015) 332-341. [PMID: 25619998]

[EC 2.3.1.257 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.257]

EC 2.3.1.258

Accepted name: N-terminal methionine Nα-acetyltransferase NatE

Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-alanyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-seryl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-valyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-threonyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-lysyl-[protein] + CoA
(6) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(7) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
(8) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA

Other name(s): NAA50 (gene name); NAT5; SAN

Systematic name: acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nα-acetyltransferase

Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nα-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase.The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hou, F., Chu, C.W., Kong, X., Yokomori, K. and Zou, H. The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. J. Cell Biol. 177 (2007) 587-597. [PMID: 17502424]

2. Pimenta-Marques, A., Tostoes, R., Marty, T., Barbosa, V., Lehmann, R. and Martinho, R.G. Differential requirements of a mitotic acetyltransferase in somatic and germ line cells. Dev. Biol. 323 (2008) 197-206. [PMID: 18801358]

3. Evjenth, R., Hole, K., Karlsen, O.A., Ziegler, M., Arnesen, T. and Lillehaug, J.R. Human Naa50p (Nat5/San) displays both protein Nα- and Nε-acetyltransferase activity. J. Biol. Chem. 284 (2009) 31122-31129. [PMID: 19744929]

4. Van Damme, P., Hole, K., Gevaert, K. and Arnesen, T. N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases. Proteomics 15 (2015) 2436-2446. [PMID: 25886145]

[EC 2.3.1.258 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.258]

EC 2.3.1.259

Accepted name: N-terminal methionine Nα-acetyltransferase NatF

Reaction: acetyl-CoA + an N-terminal-L-methionyl-[transmembrane protein] = an N-terminal-Nα-acetyl-L-methionyl-[transmembrane protein] + CoA

Other name(s): NAA60 (gene name)

Systematic name: acetyl-CoA:N-terminal-Met-Lys/Ser/Val/Leu/Gln/Ile/Tyr/Thr-[transmembrane protein] Met-Nα-acetyltransferase

Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. NatF is found only in higher eukaryotes, and is absent from yeast. Unlike other Nat systems the enzyme is located in the Golgi apparatus. It faces the cytosolic side of intracellular membranes, and specifically acetylates transmembrane proteins whose N termini face the cytosol. NatF targets N-terminal L-methionine residues attached to Lys, Ser, Val, Leu, Gln, Ile, Tyr and Thr residues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Van Damme, P., Hole, K., Pimenta-Marques, A., Helsens, K., Vandekerckhove, J., Martinho, R.G., Gevaert, K. and Arnesen, T. NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet 7 (2011) e1002169. [PMID: 21750686]

2. Aksnes, H., Van Damme, P., Goris, M., Starheim, K.K., Marie, M., Støve, S.I., Hoel, C., Kalvik, T.V., Hole, K., Glomnes, N., Furnes, C., Ljostveit, S., Ziegler, M., Niere, M., Gevaert, K. and Arnesen, T. An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. Cell Rep 10 (2015) 1362-1374. [PMID: 25732826]

[EC 2.3.1.259 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.259]

EC 2.3.1.260

Accepted name: tetracycline polyketide synthase

Reaction: malonamoyl-[OxyC acyl-carrier protein] + 8 malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + 8 CO2 + 8 CoA

For diagram of reaction click here.

Systematic name: malonyl-CoA:malonamoyl-[OxyC acyl-carrier protein] malonyltransferase

Comments: The synthesis, in the bacterium Streptomyces rimosus, of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP). Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds. Following the initiation, the PKS catalyses the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline. Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Thomas, R. and Williams, D.J. Oxytetracycline biosynthesis: origin of the carboxamide substituent. J. Chem. Soc., Chem. Commun. (1983) 677-679.

2. Zhang, W., Ames, B.D., Tsai, S.C. and Tang, Y. Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. Appl. Environ. Microbiol. 72 (2006) 2573-2580. [PMID: 16597959]

3. Yu, L., Cao, N., Wang, L., Xiao, C., Guo, M., Chu, J., Zhuang, Y. and Zhang, S. Oxytetracycline biosynthesis improvement in Streptomyces rimosus following duplication of minimal PKS genes. Enzyme Microb. Technol. 50 (2012) 318-324. [PMID: 22500899]

[EC 2.3.1.260 created 2016]

EC 2.3.1.261

Accepted name: 4-hydroxyphenylalkanoate synthase

Reaction: (1) 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase] + 8 malonyl-CoA + 16 NADPH + 16 H+ = 17-(4-hydroxyphenyl)heptadecanoyl-[4-hydroxyphenylalkanoate synthase] + 8 CO2 + 8 CoA + 16 NADP+ + 8 H2O
(2) 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase] + 9 malonyl-CoA + 18 NADPH + 18 H+ + holo-[4-hydroxyphenylalkanoate synthase] = 19-(4-hydroxyphenyl)nonadecanoyl-[4-hydroxyphenylalkanoate synthase] + 9 CO2 + 9 CoA + 18 NADP+ + 9 H2O

Other name(s): msl7 (gene name); Pks15/1

Systematic name: malonyl-CoA:4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase] malonyltransferase (4-hydroxyphenylalkanoate-forming)

Comments: The enzyme is part of the biosynthetic pathway of phenolphthiocerol, a lipid that serves as a virulence factor of pathogenic mycobacteria. It catalyses the elongation of 4-hydroxybenzoate that is loaded on its acyl-carrier domain to form 4-hydroxyphenylalkanoate intermediates. The enzyme adds either 8 or 9 malonyl-CoA units, resulting in formation of 17-(4-hydroxyphenyl)heptadecanoate or 19-(4-hydroxyphenyl)nonadecanoate, respectively. As the enzyme lacks a thioesterase domain [1], the product remains loaded on the acyl-carrier domain at the end of catalysis, and has to be hydrolysed by an as-yet unknown mechanism.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem. 276 (2001) 16833-16839. [PMID: 11278910]

2. Constant, P., Perez, E., Malaga, W., Laneelle, M.A., Saurel, O., Daffe, M. and Guilhot, C. Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the Mycobacterium tuberculosis complex. Evidence that all strains synthesize glycosylated p-hydroxybenzoic methyl esters and that strains devoid of phenolglycolipids harbor a frameshift mutation in the pks15/1 gene. J. Biol. Chem. 277 (2002) 38148-38158. [PMID: 12138124]

3. Simeone, R., Leger, M., Constant, P., Malaga, W., Marrakchi, H., Daffe, M., Guilhot, C. and Chalut, C. Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. FEBS J. 277 (2010) 2715-2725. [PMID: 20553505]

[EC 2.3.1.261 created 2017]

EC 2.3.1.262

Accepted name: anthraniloyl-CoA anthraniloyltransferase

Reaction: anthraniloyl-CoA + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CoA + CO2 (overall reaction)
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]

Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA

Other name(s): pqsD (gene name)

Systematic name: anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase

Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thiesterase, is present, it removes the CoA moiety from the product, forming the stable 2-aminobenzoylacetate.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Bera, A.K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J.P., Pesci, E.C. and Parsons, J.F. Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate. Biochemistry 48 (2009) 8644-8655. [PMID: 19694421]

2. Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481-1491. [PMID: 24239007]

3. Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611-618. [PMID: 25960261]

[EC 2.3.1.262 created 2017]

EC 2.3.1.263

Accepted name: 2-amino-4-oxopentanoate thiolase

Reaction: acetyl-CoA + D-alanine = CoA + (2R)-2-amino-4-oxopentanoate

Other name(s): AKPT; AKP thiolase; 2-amino-4-ketopentanoate thiolase

Systematic name: acetyl-CoA:D-alanine acetyltransferase

Comments: A pyridoxal 5'-phosphate enzyme. The enzyme, characterized from the bacterium Clostridium sticklandii, is part of a degradation pathway of ornithine. It is specific for acetyl-CoA and D-alanine.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Jeng, I.M., Somack, R. and Barker, H.A. Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A. Biochemistry 13 (1974) 2898-2903. [PMID: 4407783]

2. Fonknechten, N., Perret, A., Perchat, N., Tricot, S., Lechaplais, C., Vallenet, D., Vergne, C., Zaparucha, A., Le Paslier, D., Weissenbach, J. and Salanoubat, M. A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine. J. Bacteriol. 191 (2009) 3162-3167. [PMID: 19251850]

[EC 2.3.1.263 created 2017]

EC 2.3.1.264

Accepted name: β-lysine N6-acetyltransferase

Reaction: acetyl-CoA + (3S)-3,6-diaminohexanoate = CoA + (3S)-6-acetamido-3-aminohexanoate

Glossary: (3S)-3,6-diaminohexanoate = β-L-lysine
(3S)-6-acetamido-3-aminohexanoate = N6-acetyl-β-L-lysine

Other name(s): ablB (gene name)

Systematic name: acetyl-CoA:(3S)-3,6-diaminohexanoate N6-acetyltransferase

Comments: The enzyme is found in some methanogenic archaea and bacteria. In archaea it is induced under salt stress. The product, N6-acetyl-β-L-lysine, serves as a compatible solute, conferring high salt resistance on the producing organisms.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Pfluger, K., Baumann, S., Gottschalk, G., Lin, W., Santos, H. and Muller, V. Lysine-2,3-aminomutase and β-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nε-acetyl-β-lysine and growth at high salinity. Appl. Environ. Microbiol. 69 (2003) 6047-6055. [PMID: 14532061]

2. Muller, S., Hoffmann, T., Santos, H., Saum, S.H., Bremer, E. and Muller, V. Bacterial abl-like genes: production of the archaeal osmolyte N(ε)-acetyl-β-lysine by homologous overexpression of the yodP-kamA genes in Bacillus subtilis. Appl. Microbiol. Biotechnol. 91 (2011) 689-697. [PMID: 21538109]

[EC 2.3.1.264 created 2017]

EC 2.3.1.265

Accepted name: phosphatidylinositol dimannoside acyltransferase

Reaction: (1) an acyl-CoA + 2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-6-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2) an acyl-CoA + 2-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol = CoA + 2-O-(6-O-acyl-α-D-mannosyl)-1-phosphatidyl-1D-myo-inositol

Other name(s): PIM2 acyltransferase; ptfP1 (gene name)

Systematic name: acyl-CoA:2,6-di-O-α-D-mannosyl-1-phosphatidyl-1D-myo-inositol acyltransferase

Comments: The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Svetlikova, Z., Barath, P., Jackson, M., Kordulakova, J. and Mikusova, K. Purification and characterization of the acyltransferase involved in biosynthesis of the major mycobacterial cell envelope glycolipid —monoacylated phosphatidylinositol dimannoside. Protein Expr. Purif. 100 (2014) 33-39. [PMID: 24810911]

[EC 2.3.1.265 created 2017]

EC 2.3.1.266

Accepted name: [ribosomal protein S18]-alanine N-acetyltransferase

Reaction: acetyl-CoA + an N-terminal L-alanyl-[S18 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S18 protein of 30S ribosome]

Other name(s): rimI (gene name)

Systematic name: acetyl-CoA:[S18 protein of 30S ribosome]-L-alanine N-acetyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is specific for protein S18, a component of the 30S ribosomal subunit. cf. EC 2.3.1.267, [ribosomal protein S5]-alanine N-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Isono, K. and Isono, S. Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol. Gen. Genet. 177 (1980) 645-651. [PMID: 6991870]

2. Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481-488. [PMID: 2828880]

[EC 2.3.1.266 created 1990 as EC 2.3.1.128, part transferred 2018 to EC 2.3.1.266]

EC 2.3.1.267

Accepted name: [ribosomal protein S5]-alanine N-acetyltransferase

Reaction: acetyl-CoA + an N-terminal L-alanyl-[S5 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S5 protein of 30S ribosome]

Other name(s): rimJ (gene name)

Systematic name: acetyl-CoA:[S5 protein of 30S ribosome]-L-alanine N-acetyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is specific for protein S5, a component of the 30S ribosomal subunit. It also plays a role in maturation of the 30S ribosomal subunit. cf. EC 2.3.1.266, [ribosomal protein S18]-alanine N-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yoshikawa, A., Isono, S., Sheback, A. and Isono, K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12. Mol. Gen. Genet. 209 (1987) 481-488. [PMID: 2828880]

2. Roy-Chaudhuri, B., Kirthi, N., Kelley, T. and Culver, G.M. Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol. Microbiol. 68 (2008) 1547-1559. [PMID: 18466225]

3. Roy-Chaudhuri, B., Kirthi, N. and Culver, G.M. Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity. Proc. Natl. Acad. Sci. USA 107 (2010) 4567-4572. [PMID: 20176963]

[EC 2.3.1.267 created 1990 as EC 2.3.1.128, part transferred 2018 to EC 2.3.1.267]

EC 2.3.1.268

Accepted name: ethanol O-acetyltransferase

Reaction: ethanol + acetyl-CoA = ethyl acetate + CoA

Other name(s): eat1 (gene name); ethanol acetyltransferase

Systematic name: acetyl-CoA:ethanol O-acetyltransferase

Comments: The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kruis, A.J., Levisson, M., Mars, A.E., van der Ploeg, M., Garces Daza, F., Ellena, V., Kengen, S.WM., van der Oost, J. and Weusthuis, R.A. Ethyl acetate production by the elusive alcohol acetyltransferase from yeast. Metab. Eng. 41 (2017) 92-101. [PMID: 28356220]

[EC 2.3.1.268 created 2018]

EC 2.3.1.269

Accepted name: apolipoprotein N-acyltransferase

Reaction: a phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine

Other name(s): lnt (gene name); Lnt

Systematic name: phosphoglyceride:[apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine N-acyltransferase

Comments: This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Gupta, S.D. and Wu, H.C. Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. FEMS Microbiol. Lett. 62 (1991) 37-41. [PMID: 2032623]

2. Robichon, C., Vidal-Ingigliardi, D. and Pugsley, A.P. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 280 (2005) 974-983. [PMID: 15513925]

3. Hillmann, F., Argentini, M. and Buddelmeijer, N. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J. Biol. Chem. 286 (2011) 27936-27946. [PMID: 21676878]

[EC 2.3.1.269 created 2018]

EC 2.3.1.270

Accepted name: lyso-ornithine lipid O-acyltransferase

Reaction: a lyso-ornithine lipid + an acyl-[acyl-carrier protein] = an ornithine lipid + a holo-[acyl-carrier protein]

Glossary: a lyso-ornithine lipid = an Nα-[(3R)-3-hydroxyacyl]-L-ornithine
an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine

Other name(s): olsA (gene name)

Systematic name: Nα-[(3R)-hydroxy-acyl]-L-ornithine O-acyltransferase

Comments: This bacterial enzyme catalyses the second step in the formation of ornithine lipids.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Weissenmayer, B., Gao, J.L., Lopez-Lara, I.M. and Geiger, O. Identification of a gene required for the biosynthesis of ornithine-derived lipids. Mol. Microbiol. 45 (2002) 721-733. [PMID: 12139618]

2. Aygun-Sunar, S., Bilaloglu, R., Goldfine, H. and Daldal, F. Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis. J. Bacteriol. 189 (2007) 8564-8574. [PMID: 17921310]

3. Lewenza, S., Falsafi, R., Bains, M., Rohs, P., Stupak, J., Sprott, G.D. and Hancock, R.E. The olsA gene mediates the synthesis of an ornithine lipid in Pseudomonas aeruginosa during growth under phosphate-limiting conditions, but is not involved in antimicrobial peptide susceptibility. FEMS Microbiol. Lett. 320 (2011) 95-102. [PMID: 21535098]

[EC 2.3.1.270 created 2018]

EC 2.3.1.271

Accepted name: L-glutamate-5-semialdehyde N-acetyltransferase

Reaction: acetyl-CoA + L-glutamate-5-semialdehyde = CoA + N-acetyl-L-glutamate 5-semialdehyde

Other name(s): MPR1 (gene name); MPR2 (gene name)

Systematic name: acetyl-CoA:L-glutamate-5-semialdehyde N-acetyltransferase

Comments: The enzyme, characterized from the yeast Saccharomyces cerevisiae Σ1278b, N-acetylates L-glutamate-5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Shichiri, M., Hoshikawa, C., Nakamori, S. and Takagi, H. A novel acetyltransferase found in Saccharomyces cerevisiae Σ1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid. J. Biol. Chem. 276 (2001) 41998-42002. [PMID: 11555637]

2. Nomura, M. and Takagi, H. Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate. Proc. Natl Acad. Sci. USA 101 (2004) 12616-12621. [PMID: 15308773]

3. Nishimura, A., Kotani, T., Sasano, Y. and Takagi, H. An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1: oxidative stress-induced arginine synthesis and its physiological role. FEMS Yeast Res. 10 (2010) 687-698. [PMID: 20550582]

4. Nishimura, A., Nasuno, R. and Takagi, H. The proline metabolism intermediate Δ1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast. FEBS Lett. 586 (2012) 2411-2416. [PMID: 22698729]

5. Nasuno, R., Hirano, Y., Itoh, T., Hakoshima, T., Hibi, T. and Takagi, H. Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism. Proc. Natl Acad. Sci. USA 110 (2013) 11821-11826. [PMID: 23818613]

[EC 2.3.1.271 created 2018]

EC 2.3.1.272

Accepted name: 2-acetylphloroglucinol acetyltransferase

Reaction: 2 2-acetylphloroglucinol = 2,4-diacetylphloroglucinol + phloroglucinol

Glossary: phloroglucinol = benzene-1,3,5-triol

Other name(s): MAPG ATase

Systematic name: 2-acetylphloroglucinol C-acetyltransferase

Comments: The enzyme from the bacterium Pseudomonas sp YGJ3 is composed of three subunits named PhlA, PhlB and PhlC. Production of 2,4-diacetylphloroglucinol, which has antibiotic activity, is strongly inhibited by chloride ions.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Hayashi, A., Saitou, H., Mori, T., Matano, I., Sugisaki, H. and Maruyama, K. Molecular and catalytic properties of monoacetylphloroglucinol acetyltransferase from Pseudomonas sp. YGJ3. Biosci. Biotechnol. Biochem. 76 (2012) 559-566. [PMID: 22451400]

[EC 2.3.1.272 created 2018]

EC 2.3.1.273

Accepted name: diglucosylglycerate octanoyltransferase

Reaction: octanoyl-CoA + 2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate = 2-O-[6-O-octanoyl-α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate. + CoA

Other name(s): octT (gene name); DGG octanoyltransferase

Systematic name: octanoyl-CoA:2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate octanoyltransferase

Comments: The enzyme, characterized from mycobacteria, is involved in the biosynthesis of methylglucose lipopolysaccharide (MGLP). The enzyme can also act on 2-O-(α-D-glucopyranosyl)-D-glycerate, but with lower activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Maranha, A., Moynihan, P.J., Miranda, V., Correia Lourenco, E., Nunes-Costa, D., Fraga, J.S., Jose Barbosa Pereira, P., Macedo-Ribeiro, S., Ventura, M.R., Clarke, A.J. and Empadinhas, N. Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides. Sci Rep 5 (2015) 13610. [PMID: 26324178]

[EC 2.3.1.273 created 2018]

EC 2.3.1.274

Accepted name: phosphate acyltransferase

Reaction: an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein]

Other name(s): plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase

Systematic name: an acyl-[acyl-carrier protein]:phosphate acyltransferase

Comments: The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765-772. [PMID: 16949372]

2. Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7 (2007) 69. [PMID: 17645809]

3. Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157-163. [PMID: 19058030]

4. Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59-66. [PMID: 29199103]

[EC 2.3.1.274 created 2018]

EC 2.3.1.275

Accepted name: acyl phosphate:glycerol-3-phosphate acyltransferase

Reaction: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate

Other name(s): plsY (gene name); G3P acyltransferase; GPAT; lysophosphatidic acid synthase; LPA synthase

Systematic name: acyl phosphoate:sn-glycerol 3-phosphate acyltransferase

Comments: The enzyme, found in bacteria, catalyses a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. The enzyme is membrane-bound.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765-772. [PMID: 16949372]

2. Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7 (2007) 69. [PMID: 17645809]

3. Lu, Y.J., Zhang, F., Grimes, K.D., Lee, R.E. and Rock, C.O. Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. J. Biol. Chem 282 (2007) 11339-11346. [PMID: 17308305]

4. Hara, Y., Seki, M., Matsuoka, S., Hara, H., Yamashita, A. and Matsumoto, K. Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis. Genes Genet. Syst. 83 (2008) 433-442. [PMID: 19282621]

[EC 2.3.1.275 created 2018]

EC 2.3.1.276

Accepted name: galactosamine-1-phosphate N-acetyltransferase

Reaction: acetyl-CoA + α-D-galactosamine 1-phosphate = CoA + N-acetyl-α-D-galactosamine 1-phosphate

Other name(s): ST0452 (locus name)

Systematic name: acetyl-CoA:α-D-galactosamine-1-phosphate N-acetyltransferase

Comments: The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward α-D-glucosamine 1-phosphate (cf. EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase). In addition, that enzyme contains a second domain that catalyses the activities of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase, and EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Zhang, Z., Tsujimura, M., Akutsu, J., Sasaki, M., Tajima, H. and Kawarabayasi, Y. Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7. J. Biol. Chem 280 (2005) 9698-9705. [PMID: 15598657]

2. Zhang, Z., Akutsu, J. and Kawarabayasi, Y. Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7. J. Bacteriol. 192 (2010) 3287-3293. [PMID: 20400541]

3. Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]

[EC 2.3.1.276 created 2018]

EC 2.3.1.277

Accepted name: 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase

Reaction: a medium-chain 3-oxoacyl-[acyl-carrier protein] + glycerone phosphate = 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate + a holo-[acyl-carrier protein]

Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate

Other name(s): afsA (gene name); scbA (gene name); barX (gene name)

Systematic name: 3-oxoacyl-[acyl-carrier protein]:glycerone phosphate 3-oxonacylltransferase

Comments: The enzyme catalyses the first committed step in the biosynthesis of γ-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Horinouchi, S., Suzuki, H., Nishiyama, M. and Beppu, T. Nucleotide sequence and transcriptional analysis of the Streptomyces griseus gene (afsA) responsible for A-factor biosynthesis. J. Bacteriol. 171 (1989) 1206-1210. [PMID: 2492509]

2. Kato, J.Y., Funa, N., Watanabe, H., Ohnishi, Y. and Horinouchi, S. Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces. Proc. Natl Acad. Sci. USA 104 (2007) 2378-2383. [PMID: 17277085]

3. Hsiao, N.H., Soding, J., Linke, D., Lange, C., Hertweck, C., Wohlleben, W. and Takano, E. ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid synthases and is able to synthesize γ-butyrolactones. Microbiology 153 (2007) 1394-1404. [PMID: 17464053]

4. Lee, Y.J., Kitani, S. and Nihira, T. Null mutation analysis of an afsA-family gene, barX, that is involved in biosynthesis of the γ-butyrolactone autoregulator in Streptomyces virginiae. Microbiology 156 (2010) 206-210. [PMID: 19778967]

[EC 2.3.1.277 created 2018]

EC 2.3.1.278

Accepted name: mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase

Reaction: a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose = a 2-(long-chain fatty acyl)-3-mycolipenoyl-trehalose + CoA

Glossary: a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA
polyacyltrehalose = PAT = a 2-(long-chain fatty acyl)-2',3,4',6-tetramycolipenoyl-trehalose

Other name(s): papA3 (gene name)

Systematic name: mycolipenoyl-CoA:2-(long-chain-fatty acyl)-trehalose 3-mycolipenoyltransferase

Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA—trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 284 (2009) 12745-12751. [PMID: 19276083]

[EC 2.3.1.278 created 2018]

EC 2.3.1.279

Accepted name: long-chain-acyl-CoA—trehalose acyltransferase

Reaction: a long-chain fatty acyl-CoA + α,α-trehalose = a 2-(long-chain-fatty acyl)-trehalose + CoA

Glossary: polyacyltrehalose = PAT = a 2-(long-chain fatty acyl)-2',3,4',6-tetramycolipenoyl-trehalose
a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA

Other name(s): papA3 (gene name)

Systematic name: long-chain fatty acyl-CoA:α,α-trehalose 2-acyltransferase

Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 284 (2009) 12745-12751. [PMID: 19276083]

[EC 2.3.1.279 created 2018]

EC 2.3.1.280

Accepted name: (aminoalkyl)phosphonate N-acetyltransferase

Reaction: acetyl-CoA + (aminomethyl)phosphonate = CoA + (acetamidomethyl)phosphonate

Other name(s): phnO (gene name)

Systematic name: acetyl-CoA:(aminomethyl)phosphonate N-acetyltransferase

Comments: The enzyme, characterized from the bacterium Escherichia coli, is able to acetylate a range of (aminoalkyl)phosphonic acids. Requires a divalent metal ion for activity.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Errey, J.C. and Blanchard, J.S. Functional annotation and kinetic characterization of PhnO from Salmonella enterica. Biochemistry 45 (2006) 3033-3039. [PMID: 16503658]

2. Hove-Jensen, B., McSorley, F.R. and Zechel, D.L. Catabolism and detoxification of 1-aminoalkylphosphonic acids: N-acetylation by the phnO gene product. PLoS One 7 (2012) e46416. [PMID: 23056305]

[EC 2.3.1.280 created 2018]

EC 2.3.1.281

Accepted name: 5-hydroxydodecatetraenal polyketide synthase

Reaction: 6 malonyl-CoA + 5 NADPH + NADH + 6 H+ = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O

For diagram of reaction click here.

Glossary: coelimycin P1 = N-[(3R)-8-[(2E)-but-2-enoyl]-6-[(2E)-5,6-dihydropyridin-2(1H)-ylidene]-2-oxo-3,4-dihydro-2H,6H-1,5-oxathiocin-3-yl]acetamide

Other name(s): cpkABC (gene names)

Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase ((2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal-forming)

Comments: This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyses the first reaction in the biosynthesis of coelimycin P1. The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains. An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyses the reductive release of the product.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Pawlik, K., Kotowska, M., Chater, K.F., Kuczek, K. and Takano, E. A cryptic type I polyketide synthase (cpk) gene cluster in Streptomyces coelicolor A3(2). Arch. Microbiol. 187 (2007) 87-99. [PMID: 17009021]

2. Awodi, U.R., Ronan, J.L., Masschelein, J., Santos, E.LC. and Challis, G.L. Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chem. Sci. 8 (2017) 411-415. [PMID: 28451186]

[EC 2.3.1.281 created 2019]

EC 2.3.1.282

Accepted name: phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase

Reaction: (1) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol = a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase]
(2) 2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase]
(3) 2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase]

Glossary: a mycocerosate = 2,4,6-trimethyl- and 2,4,6,8-tetramethyl-2-alkanoic acids present in many pathogenic mycobacteria. The chiral centers bearing the methyl groups have an L (levorotatory) stereo configuration.
a phthiocerol = a linear carbohydrate molecule to which one methoxyl group, one methyl group, and two secondary hydroxyl groups are attached.
a phthiodiolone = an intermediate in phthiocerol biosynthesis, containing an oxo group where phthiocerols contain a methoxyl group
a phenolphthiocerol = a compound related to phthiocerol that contains a phenol group at the ω end of the molecule

Other name(s): papA5 (gene name)

Systematic name: mycocerosyl-[mycocerosic acid synthase]:phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase

Comments: The enzyme, present in certain pathogenic species of mycobacteria, catalyses the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters. The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28, which loads them onto EC 2.3.1.111, mycocerosate synthase. That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Onwueme, K.C., Ferreras, J.A., Buglino, J., Lima, C.D. and Quadri, L.E. Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapA5. Proc. Natl Acad. Sci. USA 101 (2004) 4608-4613. [PMID: 15070765]

2. Buglino, J., Onwueme, K.C., Ferreras, J.A., Quadri, L.E. and Lima, C.D. Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis. J. Biol. Chem 279 (2004) 30634-30642. [PMID: 15123643]

3. Chavadi, S.S., Onwueme, K.C., Edupuganti, U.R., Jerome, J., Chatterjee, D., Soll, C.E. and Quadri, L.E. The mycobacterial acyltransferase PapA5 is required for biosynthesis of cell wall-associated phenolic glycolipids. Microbiology 158 (2012) 1379-1387. [PMID: 22361940]

4. Touchette, M.H., Bommineni, G.R., Delle Bovi, R.J., Gadbery, J.E., Nicora, C.D., Shukla, A.K., Kyle, J.E., Metz, T.O., Martin, D.W., Sampson, N.S., Miller, W.T., Tonge, P.J. and Seeliger, J.C. Diacyltransferase activity and chain length specificity of Mycobacterium tuberculosis PapA5 in the synthesis of alkyl β-diol lipids. Biochemistry 54 (2015) 5457-5468. [PMID: 26271001]

[EC 2.3.1.282 created 2019]

EC 2.3.1.283

Accepted name: 2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase

Reaction: a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose = a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose + holo-[(hydroxy)phthioceranic acid synthase]

Other name(s): papA1 (gene name)

Systematic name: (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]:2'-acyl-2-O-sulfo-α,α-trehalose 3'-(hydroxy)phthioceranyltransferase

Comments: This mycobacterial enzyme catalyses the acylation of 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose at the 3' position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Bhatt, K., Gurcha, S.S., Bhatt, A., Besra, G.S. and Jacobs, W.R., Jr. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153 (2007) 513-520. [PMID: 17259623]

2. Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl Acad. Sci. USA 104 (2007) 11221-11226. [PMID: 17592143]

[EC 2.3.1.283 created 2019]

EC 2.3.1.284

Accepted name: 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase

Reaction: 3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-α-alpha-trehalose + 2 2'-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose

Glossary: 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-α-alpha-trehalose = a mycobacterial sulfolipid

Other name(s): chp1 (gene name)

Systematic name: 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose:3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose 6,6'-di(hydroxy)phthioceranyltransferase

Comments: The enzyme, present in mycobacteria, catalyses the ultimate step in the biosynthesis of mycobacterial sulfolipids. It catalyses two successive transfers of a (hydroxy)phthioceranyl group from two diacylated intermediates to third diacylated intermediate, generating the tetraacylated sulfolipid.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 287 (2012) 7990-8000. [PMID: 22194604]

[EC 2.3.1.284 created 2019]

EC 2.3.1.285

Accepted name: (13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase

Reaction: acetyl-CoA + (13S,14R)-1,13-dihydroxy-N-methylcanadine = (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + CoA

For diagram of reaction click here.

Other name(s): AT1 (gene name)

Systematic name: acetyl-CoA:(13S,14R)-1,13-dihydroxy-N-methylcanadine O-acetyltransferase

Comments: The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104-106. [PMID: 25485687]

2. Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl Acad. Sci. USA 115 (2018) E3922-E3931. [PMID: 29610307]

[EC 2.3.1.285 created 2019]

EC 2.3.1.286

Accepted name: protein acetyllysine N-acetyltransferase

Reaction: [protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2"-O-acetyl-ADP-D-ribose + nicotinamide (overall reaction)
(1a) [protein]-N6-acetyl-L-lysine + NAD+ = [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
(1b) [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O = [protein]-L-lysine + 2"-O-acetyl-ADP-D-ribose

Other name(s): Sir2; protein lysine deacetylase; NAD+-dependent protein deacetylase

Systematic name: [protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2"-O-acetyl-ADP-D-ribose-forming)

Comments: The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2"-O-acetyl-ADP-D-ribose converts non-enzymically to 3"-O-acetyl-ADP-D-ribose.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Landry, J., Slama, J.T. and Sternglanz, R. Role of NAD+ in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278 (2000) 685-690. [PMID: 11095969]

2. Sauve, A.A., Celic, I., Avalos, J., Deng, H., Boeke, J.D. and Schramm, V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40 (2001) 15456-15463. [PMID: 11747420]

3. Min, J., Landry, J., Sternglanz, R. and Xu, R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell 105 (2001) 269-279. [PMID: 11336676]

4. Jackson, M.D., Schmidt, M.T., Oppenheimer, N.J. and Denu, J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278 (2003) 50985-50998. [PMID: 14522996]

5. Sauve, A.A., Wolberger, C., Schramm, V.L. and Boeke, J.D. The biochemistry of sirtuins. Annu. Rev. Biochem. 75 (2006) 435-465. [PMID: 16756498]

[EC 2.3.1.286 created 2019]

EC 2.3.1.287

Accepted name: phthioceranic/hydroxyphthioceranic acid synthase

Reaction: (1) 8 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH + 16 H+ = 8 CoA + C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 16 NADP+ + 8 CO2 + 8 H2O
(2) 7 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH + 14 H+ = 7 CO2 + C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 14 NADP+ + 7 CoA + 7 H2O

Other name(s): msl2 (gene name); PKS2

Systematic name: (S)-methylmalonyl-CoA:palmitoyl-[(hydroxy)phthioceranic acid synthase] methylmalonyltransferase (phthioceranyl-[(hydroxy)phthioceranic acid synthase]-forming)

Comments: This mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions. Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively. Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem 276 (2001) 16833-16839. [PMID: 11278910]

2. Gokhale, R.S., Saxena, P., Chopra, T. and Mohanty, D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat. Prod. Rep. 24 (2007) 267-277. [PMID: 17389997]

3. Passemar, C., Arbues, A., Malaga, W., Mercier, I., Moreau, F., Lepourry, L., Neyrolles, O., Guilhot, C. and Astarie-Dequeker, C. Multiple deletions in the polyketide synthase gene repertoire of Mycobacterium tuberculosis reveal functional overlap of cell envelope lipids in host-pathogen interactions. Cell Microbiol 16 (2014) 195-213. [PMID: 24028583]

[EC 2.3.1.287 created 2019]

EC 2.3.1.288

Accepted name: 2-O-sulfo trehalose long-chain-acyltransferase

Reaction: (1) stearoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2'-stearoyl-α,α-trehalose + CoA
(2) palmitoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2'-palmitoyl-α,α-trehalose + CoA

Other name(s): papA2 (gene name)

Systematic name: acyl-CoA:2-O-sulfo-α,α-trehalose 2'-long-chain-acyltransferase

Comments: This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl Acad. Sci. USA 104 (2007) 11221-11226. [PMID: 17592143]

2. Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem 287 (2012) 7990-8000. [PMID: 22194604]

[EC 2.3.1.288 created 2019]

EC 2.3.1.289

Accepted name: aureothin polyketide synthase system

Reaction: 4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H+ = demethylluteothin + 5 CO2 + 6 CoA + 4 NADP+ + 3 H2O

For diagram of reaction, click here

Glossary: demethylluteothin = nordeoxyaureothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-hydroxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one

Other name(s): aurABC (gene names); aureothin polyketide synthase complex

Systematic name: malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethylluteothin-forming)

Comments: This polyketide synthase, characterized from the bacterium Streptomyces thioluteus, generates the backbone of the antibiotic aureothin. It is composed of 4 modules that total 18 domains and is encoded by three genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 4 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by aurA) is used twice in an iterative fashion, so that the five Claisen condensation reactions are catalysed by only four modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. He, J. and Hertweck, C. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem. Biol. 10 (2003) 1225-1232. [PMID: 14700630]

2. He, J. and Hertweck, C. Functional analysis of the aureothin iterative type I polyketide synthase. Chembiochem 6 (2005) 908-912. [PMID: 15812854]

3. Busch, B., Ueberschaar, N., Sugimoto, Y. and Hertweck, C. Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module. J. Am. Chem. Soc. 134 (2012) 12382-12385. [PMID: 22799266]

[EC 2.3.1.289 created 2019]

EC 2.3.1.290

Accepted name: spectinabilin polyketide synthase system

Reaction: 4-nitrobenzoyl-CoA + malonyl-CoA + 6 (S)-methylmalonyl-CoA + 6 NADPH + 4 H+ = demethyldeoxyspectinabilin + 7 CO2 + 8 CoA + 6 NADP+ + 5 H2O

For diagram of reaction, click here

Glossary: demethyldeoxyspectinabilin = 2-hydroxy-3,5-dimethyl-6-[(3E,5E,7E,9E)-3,5,7,9-tetramethyl-10-(4-nitrophenyl)deca-3,5,7,9-tetraen-1-yl]pyran-4-one
spectinabilin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]pyran-4-one

Other name(s): norAA’BC (gene names); spectinabilin polyketide synthase complex

Systematic name: malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethyldeoxyspectinabilin-forming)

Comments: This polyketide synthase, characterized from the bacteria Streptomyces orinoci and Streptomyces spectabilis, generates the backbone of the antibiotic spectinabilin. It is composed of 6 modules that total 28 domains and is encoded by four genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by norA) is used twice in an iterative fashion, so that the seven Claisen condensation reactions are catalysed by only six modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Traitcheva, N., Jenke-Kodama, H., He, J., Dittmann, E. and Hertweck, C. Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective. Chembiochem 8 (2007) 1841-1849. [PMID: 17763486]

2. Choi, Y.S., Johannes, T.W., Simurdiak, M., Shao, Z., Lu, H. and Zhao, H. Cloning and heterologous expression of the spectinabilin biosynthetic gene cluster from Streptomyces spectabilis. Mol. Biosyst. 6 (2010) 336-338. [PMID: 20094652]

[EC 2.3.1.290 created 2019]

EC 2.3.1.291

= Accepted name: sphingoid base N-palmitoyltransferase

Reaction: palmitoyl-CoA + a sphingoid base = a C16 ceramide + CoA

Other name(s): mammalian ceramide synthase 5; CERS5 (gene name); LASS5 (gene name)

Systematic name: palmitoyl-CoA:sphingoid base N-palmitoyltransferase

Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Lahiri, S. and Futerman, A.H. LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor. J. Biol. Chem 280 (2005) 33735-33738. [PMID: 16100120]

2. Xu, Z., Zhou, J., McCoy, D.M. and Mallampalli, R.K. LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia. J. Lipid Res. 46 (2005) 1229-1238. [PMID: 15772421]

3. Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263-271. [PMID: 15823095]

[EC 2.3.1.291 created 2019]


Continued with EC 2.3.2
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