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 2.3.1.201 to EC 2.3.1.280

Contents

EC 2.3.1.151 2,3',4,6-tetrahydroxybenzophenone synthase
EC 2.3.1.152 alcohol O-cinnamoyltransferase
EC 2.3.1.153 anthocyanin 5-(6'''-hydroxycinnamoyltransferase)
EC 2.3.1.154 transferred now EC 2.3.1.176
EC 2.3.1.155 acetyl-CoA C-myristoyltransferase
EC 2.3.1.156 phloroisovalerophenone synthase
EC 2.3.1.157 glucosamine-1-phosphate N-acetyltransferase
EC 2.3.1.158 phospholipid:diacylglycerol acyltransferase
EC 2.3.1.159 acridone synthase
EC 2.3.1.160 vinorine synthase
EC 2.3.1.161 lovastatin nonaketide synthase
EC 2.3.1.162 taxadien-5α-ol O-acetyltransferase
EC 2.3.1.163 10-hydroxytaxane O-acetyltransferase
EC 2.3.1.164 isopenicillin-N N-acyltransferase
EC 2.3.1.165 6-methylsalicylic acid synthase
EC 2.3.1.166 2α-hydroxytaxane 2-O-benzoyltransferase
EC 2.3.1.167 10-deacetylbaccatin III 10-O-acetyltransferase
EC 2.3.1.168 dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
EC 2.3.1.169 CO-methylating acetyl-CoA synthase
EC 2.3.1.170 6'-deoxychalcone synthase
EC 2.3.1.171 anthocyanin 6"-O-malonyltransferase
EC 2.3.1.172 anthocyanin 5-O-glucoside 6'''-O-malonyltransferase
EC 2.3.1.173 flavonol-3-O-triglucoside O-coumaroyltransferase
EC 2.3.1.174 3-oxoadipyl-CoA thiolase
EC 2.3.1.175 deacetylcephalosporin-C acetyltransferase
EC 2.3.1.176 propanoyl-CoA C-acyltransferase
EC 2.3.1.177 3,5-dihydroxybiphenyl synthase
EC 2.3.1.178 diaminobutyrate acetyltransferase
EC 2.3.1.179 β-ketoacyl-acyl-carrier-protein synthase II
EC 2.3.1.180 β-ketoacyl-acyl-carrier-protein synthase III
EC 2.3.1.181 lipoyl(octanoyl) transferase
EC 2.3.1.182 (R)-citramalate synthase
EC 2.3.1.183 phosphinothricin acetyltransferase
EC 2.3.1.184 acyl-homoserine-lactone synthase
EC 2.3.1.185 tropine acyltransferase
EC 2.3.1.186 pseudotropine acyltransferase
EC 2.3.1.187 acetyl-S-ACP:malonate ACP transferase
EC 2.3.1.188 ω-hydroxypalmitate O-feruloyl transferase
EC 2.3.1.189 mycothiol synthase
EC 2.3.1.190 acetoin dehydrogenase
EC 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
EC 2.3.1.192 glycine N-phenylacetyltransferase
EC 2.3.1.193 tRNAMet cytidine acetyltransferase
EC 2.3.1.194 acetoacetyl-CoA synthase
EC 2.3.1.195 (Z)-3-hexen-1-ol acetyltransferase
EC 2.3.1.196 benzyl alcohol O-benzoyltransferase
EC 2.3.1.197 dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose 3-N-acetyltransferase
EC 2.3.1.198 glycerol-3-phosphate 2-O-acyltransferase
EC 2.3.1.199 very-long-chain 3-oxoacyl-CoA synthase
EC 2.3.1.200 lipoyl amidotransferase

See the following file for:
EC 2.3.1.201 to EC 2.3.1.280

Entries

EC 2.3.1.151

Accepted name: 2,3',4,6-tetrahydroxybenzophenone synthase

Reaction: 3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2

For diagram of reaction click here.

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

Systematic name: malonyl-CoA:3-hydroxybenzoyl-CoA malonyltransferase (decarboxylating, 2,3',4,6-tetrahydroxybenzophenone-forming)

Comments: Involved in the biosynthesis of plant xanthones. Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA (cf. EC 2.3.1.220, 2,4,6-trihydroxybenzophenone synthase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 175780-21-9

References:

1. Beerhues, L. Benzophenone synthase from cultured cells of Centaurium erythraea. FEBS Lett. 383 (1996) 264-266. [PMID: 8925910]

[EC 2.3.1.151 created 1999, modified 2013]

EC 2.3.1.152

Accepted name: alcohol O-cinnamoyltransferase

Reaction: 1-O-trans-cinnamoyl-β-D-glucopyranose + ROH = alkyl cinnamate + glucose

Systematic name: 1-O-trans-cinnamoyl-β-D-glucopyranose:alcohol O-cinnamoyltransferase

Comments: acceptor alcohols (ROH) include methanol, ethanol and propanol. No cofactors are required as 1-O-trans-cinnamoyl-β-D-glucopyranose itself is an "energy-rich" (activated) acyl-donor, comparable to CoA-thioesters. 1-O-trans-Cinnamoyl-β-D-gentobiose can also act as the acyl donor, but with much less affinity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 203009-15-8

References:

1. Mock, H.-P., Strack, D. Energetics of uridine 5'-diphosphoglucose-hydroxy-cinnamic acid acyl-glucotransferase reaction. Phytochemistry 32 (1993) 575-579.

2. Latza, S., Gansser, D., Berger, R.G. Carbohydrate esters of cinnamic acid from fruits of Physalis peruviana, Psidium guajava and Vaccinium vitis IDAEA. Phytochemistry 43 (1996) 481-485.

[EC 2.3.1.152 created 1999]

EC 2.3.1.153

Accepted name: anthocyanin 5-(6'''-hydroxycinnamoyltransferase)

Reaction: 4-hydroxycinnamoyl-CoA + anthocyanidin 3,5-diglucoside = CoA + anthocyanidin 3-glucoside 5-(6-O-4-hydroxycinnamoylglucoside)

For diagram of reaction click here.

Glossary: 4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA

Systematic name: 4-hydroxycinnamoyl-CoA:anthocyanidin 3,5-diglucoside 5-O-glucoside-6'''-O-4-hydroxycinnamoyltransferase

Comments: Isolated from the plant Gentiana triflora. Transfers the hydroxycinnamoyl group only to the C-5 glucoside of anthocyanin. Caffeoyl-CoA, but not malonyl-CoA, can substitute as an acyl donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 198841-53-1

References:

1. Fujiwara, H., Tanaka, Y., Fukui, Y., Nakao, M., Ashikari, T., Kusumi, T. Anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Purification, characterization and its role in anthocyanin biosynthesis. Eur. J. Biochem. 249 (1997) 45-51. [PMID: 9363752]

2. Fujiwara, H., Tanaka, Y., Yonekura-Sakakibara, K., Fukuchi-Mizutani, M., Nakao, M., Fukui, Y., Yamaguchi, M., Ashikari, T. and Kusumi, T. cDNA cloning, gene expression and subcellular localization of anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Plant J. 16 (1998) 421-431. [PMID: 9881162]

[EC 2.3.1.153 created 1999, modified 2013]

[EC 2.3.1.154 Transferred entry: Propionyl-CoA C2-trimethyltridecanoyltransferase. Now EC 2.3.1.176, propanoyl-CoA C-acyltransferase. (EC 2.3.1.154 created 2000, deleted 2015)]

EC 2.3.1.155

Accepted name: acetyl-CoA C-myristoyltransferase

Reaction: myristoyl-CoA + acetyl-CoA = CoA + 3-oxopalmitoyl-CoA

Other name: 3-oxopalmitoyl-CoA hydrolase; 3-oxopalmitoyl-CoA-CoA acetyltransferase

Systematic name: myristoyl-CoA:acetyl-CoA C-myristoyltransferase

Comments: A peroxisomal enzyme involved in branched chain fatty acid β-oxidation in peroxisomes. It differs from EC 2.3.1.154 (propionyl-CoA C2-trimethyldecanoyltransferase) in not being active towards 3-oxopristanoyl-CoA.

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

References:

1. Miyazawa, S., Furuta, S., Osumi, T., Hashimoto, T. and Ui, N. Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver. J Biochem (Tokyo) 90 (1981) 511-519. [PMID: 6117552]

[EC 2.3.1.155 created 2000]

EC 2.3.1.156

Accepted name: phloroisovalerophenone synthase

Reaction: isovaleryl-CoA + 3 malonyl-CoA = 4 CoA + 3 CO2 + 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one

For diagram of reaction click here.

Other name(s): valerophenone synthase; 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase

Systematic name: isovaleryl-CoA:malonyl-CoA acyltransferase

Comments: Closely related to EC 2.3.1.74, naringenin-chalcone synthase. The product, 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one, is phloroisovalerophenone. Also acts on isobutyryl-CoA as substrate to give phlorisobutyrophenone. The products are intermediates in the biosynthesis of the bitter (α) acids in hops (Humulus lupulus).

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

References:

1. Fung, S.Y., Zuurbier, K.W.M., Paniego, N.B., Scheffer, J.J.C. and Verpoorte, R. Enzymes from the biosynthesis of hop α and β acids. Proc. 26th Congr. Eur. Brew. Conv. (1997) 215-221.

2. Zuurbier, K.W.M., Leser, J., Berger, T., Hofte, A.J.P., Schroder, G., Verpoorte, R. and Schroder, J. 4-Hydroxy-2-pyrone formation by chalcone and stilbene synthase with nonphysiological substrates. Phytochemistry 49 (1998) 1945-1951.

[EC 2.3.1.156 created 2000]

EC 2.3.1.157

Accepted name: glucosamine-1-phosphate N-acetyltransferase

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

For diagram click here.

Other Name(s): acetyl-CoA:D-glucosamine-1-phosphate N-acetyltransferase

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

Comments: The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-91-8

References:

1. Mengin-Lecreulx, D. and van Heijenoort, J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176: (1994) 5788-5795. [PMID: 8083170]

2. Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35 (1996) 579-585. [PMID: 8555230]

3. Olsen, L.R. and Roderick, S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40 (2001) 1913-1921. [PMID: 11329257]

[EC 2.3.1.157 created 2001]

EC 2.3.1.158

Accepted name: phospholipid:diacylglycerol acyltransferase

Reaction: phospholipid + 1,2-diacyl-sn-glycerol = lysophospholipid + triacylglycerol

Glossary entries:
ricinoleic acid = (9Z,12R)-12-hydroxyoctadec-9-enoic acid
vernolic acid = (9Z,12S,13R)-12,13-epoxyoctadec-9-enoic acid.

Other name(s): PDAT

Systematic name: phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase

Comments: This enzyme differs from EC 2.3.1.20, diacylglycerol O-acyltransferase, by synthesising triacylglycerol using an acyl-CoA-independent mechanism. The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk's beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 288587-47-3

References:

1. Dahlqvist, A., Stähl, U., Lenman, M., Banas, A., Lee, M., Sandager, L., Ronne, H. and Stymne, S. Phospholipid:diacylglycerol acyltransferase: An enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc. Natl. Acad. Sci. USA 97 (2000) 6487-6492. [PMID: 10829075]

[EC 2.3.1.158 created 2001]

EC 2.3.1.159

Accepted name: acridone synthase

Reaction: 3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2

For diagram click here.

Systematic name: malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing)

Comments: Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99085-53-7

References:

1. Baumert, A., Maier, W., Gröger, D. and Deutzmann, R. Purification and properties of acridone synthase from cell suspension cultures of Ruta graveolens L. Z. Naturforsch. C: Biosci. 49 (1994) 26-32. [PMID: 8148006]

2. Maier, W., Baumert, A., Schumann, B., Furukawa, H. and Gröger, D. Synthesis of 1,3-dihydroxy-N-methylacridone and its conversion to rutacridone by cell-free extracts of Ruta-graveolens cell cultures. Phytochemistry 32 (1993) 691-698.

3. Lukacin. R., Springob, K., Urbanke, C., Ernwein, C., Schröder, G., Schröder, J. and Matern, U. Native acridone synthases I and II from Ruta graveolens L. form homodimers. FEBS Lett. 448 (1999) 135-140. [PMID: 10217426]

4. Junghanns, K.T., Kneusel, R.E., Groger, D. and Matern, U. Differential regulation and distribution of acridone synthase in Ruta graveolens. Phytochemistry 49 (1998) 403-411. [PMID: 9747538]

[EC 2.3.1.159 created 2002]

EC 2.3.1.160

Accepted name: vinorine synthase

Reaction: acetyl-CoA + 16-epivellosimine = CoA + vinorine

For diagram click here.

Systematic name: acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing)

Comments: The reaction proceeds in two stages. The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring. This alcohol is then acetylated. Also acts on gardneral (11-methoxy-16-epivellosimine). Generates the ajmalan skeleton, which forms part of the route to ajmaline.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 88844-97-7

References:

1. Pfitzner, A., Polz, L. and Stöckligt, J. Properties of vinorine synthase the Rauwolfia enzyme involved in the formation of the ajmaline skeleton. Z. Naturforsch. C: Biosci. 41 (1986) 103-114.

2. Bayer, A., Ma, X. and Stöckigt, J. Acetyltransfer in natural product biosynthesis—functional cloning and molecular analysis of vinorine synthase. Bioorg. Med. Chem. 12 (2004) 2787-2795. [PMID: 15110860]

3. Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., Michel, H. and Stöckigt, J. Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochim. Biophys. Acta 1701 (2004) 129-132. [PMID: 15450182]

4. Ma, X., Koepke, J., Panjikar, S., Fritzsch, G. and Stöckigt, J. Crystal structure of vinorine synthase, the first representative of the BAHD superfamily. J. Biol. Chem. 280 (2005) 13576-13583. [PMID: 15665331]

[EC 2.3.1.160 created 2002]

EC 2.3.1.161

Accepted name: lovastatin nonaketide synthase

Reaction: 9 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O

For diagram of reaction click here.

Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate

Other name(s): LNKS; LovB; LovC; acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing)

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (dihydromonacolin L acid-forming)

Comments: This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 235426-97-8

References:

1. Ma, S.M., Li, J.W., Choi, J.W., Zhou, H., Lee, K.K., Moorthie, V.A., Xie, X., Kealey, J.T., Da Silva, N.A., Vederas, J.C. and Tang, Y. Complete reconstitution of a highly reducing iterative polyketide synthase. Science 326 (2009) 589-592. [PMID: 19900898]

2. 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]

3. Auclair, K., Sutherland, A., Kennedy, J., Witter, D.J., van der Heever, J.P., Hutchinson, C.R. and Vederas, J.C. Lovastatin nonaketide synthase catalyses an intramolecular Diels-Alder reaction of a substrate analogue. J. Am. Chem. Soc. 122 (2000) 11519-11520.

[EC 2.3.1.161 created 2002, modified 2015, modified 2016]

EC 2.3.1.162

Accepted name: taxadien-5α-ol O-acetyltransferase

Reaction: acetyl-CoA + taxa-4(20),11-dien-5α-ol = CoA + taxa-4(20),11-dien-5α-yl acetate

For diagram click here.

Other name(s): acetyl coenzyme A:taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase

Systematic name: acetyl-CoA:taxa-4(20),11-dien-5α-ol O-acetyltransferase

Comments: This is the third enzyme in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel), which is widely used in the treatment of carcinomas, sarcomas and melanomas.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 229032-29-5

References:

1. Walker, K., Ketchum, R.E., Hezari, M., Gatfield, D., Goleniowski, M., Barthol, A. and Croteau, R. Partial purification and characterization of acetyl coenzyme A: taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis. Arch. Biochem. Biophys. 364 (1999) 273-9. [PMID: 10190984]

2. Walker, K., Schoendorf, A. and Croteau, R. Molecular cloning of a taxa-4(20),11(12)-dien-5α-ol-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Arch. Biochem. Biophys. 374 (2000) 371-380. [PMID: 10666320]

[EC 2.3.1.162 created 2002]

EC 2.3.1.163

Accepted name: 10-hydroxytaxane O-acetyltransferase

Reaction: acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C

For diagram click here.

Other name(s): acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase

Systematic name: acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments: Acts on a number of related taxane diterpenoids with a free 10β-hydroxy group. May be identical to EC 2.3.1.167, 10-deacetylbaccatin III 10-O-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 220946-63-4

References:

1. Menhard, B. and Zenk, M.H. Purification and characterization of acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis. Phytochemistry 50 (1999) 763-74. [PMID: 10192963]

[EC 2.3.1.163 created 2002]

EC 2.3.1.164

Accepted name: isopenicillin-N N-acyltransferase

Reaction: phenylacetyl-CoA + isopenicillin N + H2O = CoA + penicillin G + L-2-aminohexanedioate

For diagram click here.

Other name(s): acyl-coenzyme A:isopenicillin N acyltransferase; isopenicillin N:acyl-CoA: acyltransferase

Systematic name: acyl-CoA:isopenicillin N N-acyltransferase

Comments: Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 54576-90-8

References:

1. Tobin, M.B., Fleming, M.D., Skatrud, P.L. and Miller, J.R. Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli. J. Bacteriol. 172 (1990) 5908-5914. [PMID: 2120195]

2. Aplin, R.T., Baldwin, J.E., Roach, P.L., Robinson, C.V. and Schofield, C.J. Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry. Biochem. J. 294 (1993) 357-363. [PMID: 8396910 ]

[EC 2.3.1.164 created 2002]

EC 2.3.1.165

Accepted name: 6-methylsalicylic acid synthase

Reaction: acetyl-CoA + 3 malonyl-CoA + NADPH + H+ = 6-methylsalicylate + 4 CoA + 3 CO2 + NADP+ + H2O

For diagram of reaction click here.

Other name(s): MSAS; 6-methylsalicylic acid synthase

Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl-reducing, thioester-hydrolysing and cyclizing)

Comments: A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein. It has a similar sequence to vertebrate type I fatty acid synthase. Acetoacetyl-CoA can also act as a starter molecule.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9045-37-8

References:

1. Spencer, J.B. and Jordan, P.M. Purification and properties of 6-methylsalicylic acid synthase from Penicillium patulum. Biochem. J. 288 (1992) 839-846. [PMID: 1471999]

2. Child, C.J., Spencer, J.B., Bhogal, P. and Shoolingin-Jordan, P.M. Structural similarities between 6-methylsalicylic acid synthase from Penicillium patulum and vertebrate type I fatty acid synthase: evidence from thiol modification studies.Biochemistry 35 (1996) 12267-74 [PMID: 8823160]

3. Richardson, M.T., Pohl, N.L., Kealey, J.T. and Khosla, C. Tolerance and specificity of recombinant 6-methylsalicyclic acid synthase. Metab. Eng. 1 (1999) 180-187. [PMID: 10935930]

[EC 2.3.1.165 created 2002]

EC 2.3.1.166

Accepted name: 2α-hydroxytaxane 2-O-benzoyltransferase

Reaction: benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA + 10-deacetylbaccatin III

For diagram click here.

Other name(s): benzoyl-CoA:taxane 2α-O-benzoyltransferase

Systematic name: benzoyl-CoA:taxan-2α-ol O-benzoyltransferase

Comments: The enzyme was studied using the semisynthetic substrate 2-debenzoyl-7,13-diacetylbaccatin III. It will not acylate the hydroxy group at 1β, 7β, 10β or 13α of 10-deacetyl baccatin III, or at 2α or 5α of taxa-4(20),11-diene-2α,5α-diol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 329318-50-5

References:

1. Walker, K. and Croteau, R. Taxol biosynthesis: molecular cloning of a benzoyl-CoA:taxane 2α-O-benzoyltransferase cDNA from taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 13591-135916 [PMID: 11095755]

[EC 2.3.1.166 created 2002]

EC 2.3.1.167

Accepted name: 10-deacetylbaccatin III 10-O-acetyltransferase

Reaction: acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III

For diagram click here.

Systematic name: acetyl-CoA:taxan-10β-ol O-acetyltransferase

Comments: The enzyme will not acylate the hydroxy group at 1β, 7β or 13α of 10-deacetyl baccatin III, or at 5α of taxa-4(20),11-dien-5α-ol. May be identical to EC 2.3.1.163, 10-hydroxytaxane O-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 220946-63-4

References:

1. Walker. K and Croteau, R. Molecular cloning of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 97 (2000) 583-587 [PMID: 10639122]

[EC 2.3.1.167 created 2002]

EC 2.3.1.168

Accepted name: dihydrolipoyllysine-residue (2-methylpropanoyl)transferase

Reaction: 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine

For diagram of reaction click here.

Glossary: dihydrolipoyl group

Other name(s): dihydrolipoyl transacylase

Systematic name: 2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase

Comments: A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 102784-26-9

References:

1. Massey, L.K., Sokatch, J.R. and Conrad, R.S. Branched-chain amino acid catabolism in bacteria. Bacteriol. Rev. 40 (1976) 42-54. [PMID: 773366]

2. Chuang, D.T., Hu, C.C., Ku, L.S., Niu, W.L., Myers, D.E. and Cox R.P. Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase. J. Biol. Chem. 259 (1984) 9277-9284. [PMID: 6746648]

3. Wynn, R.M., Davie, J.R., Zhi, W., Cox, R.P. and Chuang, D.T. In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES. Biochemistry 33 (1994) 8962-8968. [PMID: 7913832]

4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

[EC 2.3.1.168 created 2003]

EC 2.3.1.169

Accepted name: CO-methylating acetyl-CoA synthase

Reaction: acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]

Systematic name: acetyl-CoA:corrinoid protein O-acetyltransferase

Comments: Contains nickel, copper and iron-sulfur clusters. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 176591-19-8

References:

1. Ragsdale, S.W. and Wood, H.G. Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. J. Biol. Chem. 260 (1985) 3970-3977. [PMID: 2984190]

2. Doukov, T.I., Iverson, T., Seravalli, J., Ragsdale, S.W. and Drennan, C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567-572. [PMID: 12386327]

[EC 2.3.1.169 created 2003, modified 2015]

EC 2.3.1.170

Accepted name: 6'-deoxychalcone synthase

Reaction: 3 malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ = 4 CoA + isoliquiritigenin + 3 CO2 + NADP+ + H2O

For diagram click here.

Glossary: isoliquiritigenin = 4,2',4'-trihydroxychalcone
liquiritigenin = 7,4'-dihydroxyflavanone

Systematic name: malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing, reducing)

Comments: Isoliquiritigenin is the precursor of liquiritigenin, a 5-deoxyflavanone.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114308-23-5

References:

1. Ayabe, S., Udagawa, A. and Furuya, T. NAD(P)H-dependent 6'-deoxychalcone synthase activity in Glycyrrhiza echinata cells induced by yeast extract. Arch. Biochem. Biophys. 261 (1988) 458-462. [PMID: 3355160]

[EC 2.3.1.170 created 2004]

EC 2.3.1.171

Accepted name: anthocyanin 6"-O-malonyltransferase

Reaction: malonyl-CoA + an anthocyanidin 3-O-β-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-β-D-glucoside)

For diagram click here.

Other Name(s): Dv3MaT; malonyl-coenzymeA:anthocyanidin-3-O-β-D-glucoside 6"-O-malonyltransferase; 3MaT

Systematic name: malonyl-CoA:anthocyanidin-3-O-β-D-glucoside 6"-O-malonyltransferase

Comments: Acts on pelargonidin 3-O-glucoside in dahlia (Dahlia variabilis), delphinidin 3-O-glucoside, and on cyanidin 3-O-glucoside in transgenic petunia (Petunia hybrida).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 111070-07-6

References:

1. Suzuki, H., Nakayama, T., Yonekura-Sakakibara, K., Fukui, Y., Nakamura, N., Yamaguchi, M.A., Tanaka, Y., Kusumi, T. and Nishino, T. cDNA cloning, heterologous expressions, and functional characterization of malonyl-coenzyme A:anthocyanidin 3-O-glucoside-6"-O-malonyltransferase from dahlia flowers. Plant Physiol. 130 (2002) 2142-2151. [PMID: 12481098]

[EC 2.3.1.171 created 2004]

EC 2.3.1.172

Accepted name: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase

Reaction: malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-β-D-glucoside = CoA + 4'''-demalonylsalvianin

For diagram 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)
pelargonidin = 3,4′,5,7-tetrahydroxyflavylium

Other Name(s): Ss5MaT1

Systematic name: malonyl-CoA:pelargonidin-3-O-(6-caffeoyl-β-D-glucoside)-5-O-β-D-glucoside 6'''-O-malonyltransferase

Comments: Specific for the penultimate step in salvianin biosynthesis. The enzyme also catalyses the malonylation of shisonin to malonylshisonin [cyanidin 3-O-(6"-O-p-coumaryl-β-D-glucoside)-5-(6'''-O-malonyl-β-D-glucoside)]. The compounds 4'''-demalonylsalvianin, salvianin, pelargonidin 3,5-diglucoside and delphinidin 3,5-diglucoside cannot act as substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 380229-66-3

References:

1. Suzuki, H., Nakayama, T., Yonekura-Sakakibara, K., Fukui, Y., Nakamura, N., Nakao, M., Tanaka, Y., Yamaguchi, M.A., Kusumi, T. and Nishino, T. Malonyl-CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase from scarlet sage (Salvia splendens) flowers. J. Biol. Chem. 276 (2001) 49013-49019. [PMID: 11598135]

[EC 2.3.1.172 created 2004]

EC 2.3.1.173

Accepted name: flavonol-3-O-triglucoside O-coumaroyltransferase

Reaction: 4-coumaroyl-CoA + a flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] = CoA + a flavonol 3-O-[6-(4-coumaroyl)-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside]

For diagram click here.

Other name(s): 4-coumaroyl-CoA:flavonol-3-O-[β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase (incorrect); 4-coumaroyl-CoA:flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase

Systematic name: 4-coumaroyl-CoA:flavonol 3-O-(β-D-glucosyl-1,2-β-D-glucosyl-1,2-β-D-glucoside) 6'''-O-4-coumaroyltransferase

Comments: Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64972-79-8

References:

1. Saylor, M.H. and Mansell, R.L. Hydroxycinnamoyl:coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p-coumaroyl triglucoside) in Pisum sativum. Z. Naturforsch. [C] 32 (1977) 765-768. [PMID: 145116]

[EC 2.3.1.173 created 2004]

EC 2.3.1.174

Accepted name: 3-oxoadipyl-CoA thiolase

Reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA

For diagram of reaction click here or click here or click here.

Systematic name: succinyl-CoA:acetyl-CoA C-succinyltransferase

Comments: The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223 (3-oxo-5,6-dehydrosuberyl-CoA thiolase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 403496-07-1

References:

1. Kaschabek, S.R., Kuhn, B., Müller, D., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 207-215. [PMID: 11741862]

2. Gobel, M., Kassel-Cati, K., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 216-223. [PMID: 11741863]

3. 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 2.3.1.174 created 2005, modified 2013]

EC 2.3.1.175

Accepted name: deacetylcephalosporin-C acetyltransferase

Reaction: acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C

For diagram click here.

Other name(s): acetyl-CoA:deacetylcephalosporin-C acetyltransferase; DAC acetyltransferase; cefG; deacetylcephalosporin C acetyltransferase; acetyl coenzyme A:DAC acetyltransferase; acetyl-CoA:DAC acetyltransferase; CPC acetylhydrolase; acetyl-CoA:DAC O-acetyltransferase; DAC-AT

Systematic name: acetyl-CoA:deacetylcephalosporin-C O-acetyltransferase

Comments: This enzyme catalyses the final step in the biosynthesis of cephalosporin C.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 57827-76-6

References:

1. Matsuyama, K., Matsumoto, H., Matsuda, A., Sugiura, H., Komatsu, K. and Ichikawa, S. Purification of acetyl coenzyme A: deacetylacephalosporin C O-acetyltransferase from Acremonium chrysogenum. Biosci. Biotechnol. Biochem. 56 (1992) 1410-1412. [PMID: 1368946]

2. Gutiérrez, S., Velasco, J., Fernandez, F.J. and Martín, J.F. The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and encodes a deacetylcephalosporin C acetyltransferase closely related to homoserine O-acetyltransferase. J. Bacteriol. 174 (1992) 3056-3064. [PMID: 1569032]

3. Matsuda, A., Sugiura, H., Matsuyama, K., Matsumoto, H., Ichikawa, S. and Komatsu, K. Cloning and disruption of the cefG gene encoding acetyl coenzyme A: deacetylcephalosporin C O-acetyltransferase from Acremonium chrysogenum. Biochem. Biophys. Res. Commun. 186 (1992) 40-46. [PMID: 1632779]

4. Gutiérrez, S., Velasco, J., Marcos, A.T., Fernández, F.J., Fierro, F., Barredo, J.L., Díez, B. and Martín, J.F. Expression of the cefG gene is limiting for cephalosporin biosynthesis in Acremonium chrysogenum. Appl. Microbiol. Biotechnol. 48 (1997) 606-614. [PMID: 9421924]

5. Velasco, J., Gutierrez, S., Campoy, S. and Martin, J.F. Molecular characterization of the Acremonium chrysogenum cefG gene product: the native deacetylcephalosporin C acetyltransferase is not processed into subunits. Biochem. J. 337 (1999) 379-385. [PMID: 9895280]

6. Martín, J.F., Gutiérrez, S., Fernández, F.J., Velasco, J., Fierro, F., Marcos, A.T. and Kosalkova, K. Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins. Antonie Van Leeuwenhoek 65 (1994) 227-43. [PMID: 7847890]

[EC 2.3.1.175 created 2005]

EC 2.3.1.176

Accepted name: propanoyl-CoA C-acyltransferase

Reaction: 3α,7α,12α-trihydroxy-5β-cholanoyl-CoA + propanoyl-CoA = CoA + 3α,7α,12α-trihydroxy-24-oxo-5β-cholestanoyl-CoA

For diagram click here.

Other name(s): peroxisomal thiolase 2; sterol carrier protein-χ; SCPχ; PTE-2 (ambiguous)

Systematic name: 3α,7α,12α-trihydroxy-5β-cholanoyl-CoA:propanoyl-CoA C-acyltransferase

Comments: Also acts on dihydroxy-5β-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase [4].

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

References:

1. Pedersen, J.I. and Gustafsson, J. Conversion of 3α,7α,12α-trihydroxy-5β-cholestanoic acid into cholic acid by rat liver peroxisomes. FEBS Lett. 121 (1980) 345-348. [PMID: 7461136]

2. Kase, F., Björkhem, I. and Pedersen, J.I. Formation of cholic acid from 3α,7α,12α-trihydroxy-5β-cholestanoic acid by rat liver peroxisomes. J. Lipid Res. 24 (1983) 1560-1567. [PMID: 6668450]

3. Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137-174. [PMID: 12543708]

4. Falany, C.N., Johnson, M.R., Barnes, S. and Diasio, R.B. Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J. Biol. Chem. 269 (1994) 19375-19379. [PMID: 8034703]

[EC 2.3.1.176 created 2005]

EC 2.3.1.177

Accepted name: 3,5-dihydroxybiphenyl synthase

Reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2

For diagram of reaction click here.

Other name(s): BIS1; biphenyl synthase (ambiguous)

Systematic name: malonyl-CoA:benzoyl-CoA malonyltransferase

Comments: A polyketide synthase that is involved in the production of the phytoalexin aucuparin. 2-Hydroxybenzoyl-CoA can also act as substrate but it leads to the derailment product 4-hydroxycoumarin (cf. EC 2.3.1.208, 4-hydroxycoumarin synthase) [2]. This enzyme uses the same starter substrate as EC 2.3.1.151, benzophenone synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 1217551-24-0

References:

1. Liu, B., Beuerle, T., Klundt, T. and Beerhues, L. Biphenyl synthase from yeast-extract-treated cell cultures of Sorbus aucuparia. Planta 218 (2004) 492-496. [PMID: 14595561]

2. Liu, B., Raeth, T., Beuerle, T. and Beerhues, L. Biphenyl synthase, a novel type III polyketide synthase. Planta 225 (2007) 1495-1503. [PMID: 17109150]

[EC 2.3.1.177 created 2006, modified 2012]

EC 2.3.1.178

Accepted name: diaminobutyrate acetyltransferase

Reaction: acetyl-CoA + L-2,4-diaminobutanoate = CoA + (2S)-4-acetamido-2-aminobutanoate

For diagram, click here

Other name(s): L-2,4-diaminobutyrate acetyltransferase; L-2,4-diaminobutanoate acetyltransferase; EctA; diaminobutyric acid acetyltransferase; DABA acetyltransferase; 2,4-diaminobutanoate acetyltransferase; DAB acetyltransferase; DABAcT

Systematic name: acetyl-CoA:L-2,4-diaminobutanoate N4-acetyltransferase

Comments: Requires Na+ or K+ for maximal activity [3]. Ornithine, lysine, aspartate, and α-, β- and γ-aminobutanoate cannot act as substrates [3]. However, acetyl-CoA can be replaced by propanoyl-CoA, although the reaction proceeds more slowly [3]. Forms part of the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.6.1.76, diaminobutyrate—2-oxoglutarate transaminase and EC 4.2.1.108, ectoine synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 130456-92-7

References:

1. Peters, P., Galinski, E.A. and Truper, H.G. The biosynthesis of ectoine. FEMS Microbiol. Lett. 71 (1990) 157-162.

2. Ono, H., Sawada, K., Khunajakr, N., Tao, T., Yamamoto, M., Hiramoto, M., Shinmyo, A., Takano, M. and Murooka, Y. Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata. J. Bacteriol. 181 (1999) 91-99. [PMID: 9864317]

3. Reshetnikov, A.S., Mustakhimov, I.I., Khmelenina, V.N. and Trotsenko, Y.A. Cloning, purification, and characterization of diaminobutyrate acetyltransferase from the halotolerant methanotroph Methylomicrobium alcaliphilum 20Z. Biochemistry (Mosc.) 70 (2005) 878-883. [PMID: 16212543]

4. Kuhlmann, A.U. and Bremer, E. Osmotically regulated synthesis of the compatible solute ectoine in Bacillus pasteurii and related Bacillus spp. Appl. Environ. Microbiol. 68 (2002) 772-783. [PMID: 11823218]

5. Louis, P. and Galinski, E.A. Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli. Microbiology 143 (1997) 1141-1149. [PMID: 9141677]

[EC 2.3.1.178 created 2006]

EC 2.3.1.179

Accepted name: β-ketoacyl-acyl-carrier-protein synthase II

Reaction: a (Z)-hexadec-11-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadeca-13-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]

Other name(s): KASII; KAS II; FabF; 3-oxoacyl-acyl carrier protein synthase I; β-ketoacyl-ACP synthase II

Glossary: palmitoleoyl-[acyl-carrier protein] = (Z)-hexadec-11-enoyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] = (Z)-octadeca-13-enoyl-[acyl-carrier protein]

Systematic name: (Z)-hexadec-11-enoyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)

Comments: Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, β-ketoacyl-ACP synthase I, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme [1,2]. The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. This enzyme controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures [3,4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1048648-42-5

References:

1. D'Agnolo, G., Rosenfeld, I.S. and Vagelos, P.R. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250 (1975) 5289-5294. [PMID: 237914]

2. Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr.. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. J. Biol. Chem. 255 (1980) 11949-11956. [PMID: 7002930]

3. Price, A.C., Rock, C.O. and White, S.W. The 1.3-Angstrom-resolution crystal structure of β-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae. J. Bacteriol. 185 (2003) 4136-4143. [PMID: 12837788]

4. Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr. β-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis. J. Biol. Chem. 255 (1980) 3263-3265. [PMID: 6988423]

5. Magnuson, K., Carey, M.R. and Cronan, J.E., Jr. The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene. J. Bacteriol. 177 (1995) 3593-3595. [PMID: 7768872]

6. Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612-636.

[EC 2.3.1.179 created 2006]

EC 2.3.1.180

Accepted name: β-ketoacyl-acyl-carrier-protein synthase III

Reaction: acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2

Other name(s): 3-oxoacyl:ACP synthase III; 3-ketoacyl-acyl carrier protein synthase III; KASIII; KAS III; FabH; β-ketoacyl-acyl carrier protein synthase III; β-ketoacyl-ACP synthase III; β-ketoacyl (acyl carrier protein) synthase III

Systematic name: acetyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase

Comments: Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41 (β-ketoacyl-ACP synthase I) and EC 2.3.1.179 (β-ketoacyl-ACP synthase II), this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer [1]. In addition to the above reaction, the enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent [1]. The enzyme is responsible for initiating both straight- and branched-chain fatty-acid biosynthesis [2], with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism [2,5]. For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4—C6) acyl-CoA primers [3] whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA [4,5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1048646-78-1

References:

1. Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 (1992) 6807-6814. [PMID: 1551888]

2. Han, L., Lobo, S. and Reynolds, K.A. Characterization of β-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis. J. Bacteriol. 180 (1998) 4481-4486. [PMID: 9721286]

3. Khandekar, S.S., Gentry, D.R., Van Aller, G.S., Warren, P., Xiang, H., Silverman, C., Doyle, M.L., Chambers, P.A., Konstantinidis, A.K., Brandt, M., Daines, R.A. and Lonsdale, J.T. Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae β-ketoacyl-acyl carrier protein synthase III (FabH). J. Biol. Chem. 276 (2001) 30024-30030. [PMID: 11375394]

4. Choi, K.H., Kremer, L., Besra, G.S. and Rock, C.O. Identification and substrate specificity of β-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J. Biol. Chem. 275 (2000) 28201-28207. [PMID: 10840036]

5. Qiu, X., Choudhry, A.E., Janson, C.A., Grooms, M., Daines, R.A., Lonsdale, J.T. and Khandekar, S.S. Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Protein Sci. 14 (2005) 2087-2094. [PMID: 15987898]

6. Li, Y., Florova, G. and Reynolds, K.A. Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH). J. Bacteriol. 187 (2005) 3795-3799. [PMID: 15901703]

7. Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612-636.

[EC 2.3.1.180 created 2006]

EC 2.3.1.181

Accepted name: lipoyl(octanoyl) transferase

Reaction: an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]

Glossary: lipoyl group

Other name(s): LipB; lipoyl (octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase; lipoyl (octanoyl)-acyl carrier protein:protein transferase; lipoate/octanoate transferase; lipoyltransferase; octanoyl-[acyl carrier protein]-protein N-octanoyltransferase; lipoyl(octanoyl)transferase; octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase

Systematic name: octanoyl-[acyl-carrier protein]:protein N-octanoyltransferase

Comments: This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate [4] although octanoyl-ACP is likely to be the true substrate [6] . The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate—protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 392687-64-8

References:

1. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269-282. [PMID: 15642479]

2. Vanden Boom, T.J., Reed, K.E. and Cronan, J.E., Jr. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J. Bacteriol. 173 (1991) 6411-6420. [PMID: 1655709]

3. Jordan, S.W. and Cronan, J.E., Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903-17906. [PMID: 9218413]

4. Zhao, X., Miller, J.R., Jiang, Y., Marletta, M.A. and Cronan, J.E. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem. Biol. 10 (2003) 1293-1302. [PMID: 14700636]

5. Wada, M., Yasuno, R., Jordan, S.W., Cronan, J.E., Jr. and Wada, H. Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell Physiol. 42 (2001) 650-656. [PMID: 11427685]

6. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

[EC 2.3.1.181 created 2006, modified 2016]

EC 2.3.1.182

Accepted name: (R)-citramalate synthase

Reaction: acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate

Glossary: (–)-citramalate = (2R)-2-methylmalate = (2R)-2-hydroxy-2-methylbutanedioate
α-ketoisovalerate = 3-methyl-2-oxobutanoate
α-ketobutyrate = 2-oxobutanoate
α-ketoisocaproate = 4-methyl-2-oxopentanoate
α-ketopimelate = 2-oxohexanoate
α-ketoglutarate = 2-oxoglutarate

Other name(s): CimA

Comments: One of the enzymes involved in a novel pyruvate pathway for isoleucine biosynthesis that is found in some, mainly archaeal, bacteria [1,2]. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine [2]. The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2].

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

References:

1. Howell, D.M., Xu, H. and White, R.H. (R)-Citramalate synthase in methanogenic archaea. J. Bacteriol. 181 (1999) 331-333. [PMID: 9864346]

2. Xu, H., Zhang, Y., Guo, X., Ren, S., Staempfli, A.A., Chiao, J., Jiang, W. and Zhao, G. Isoleucine biosynthesis in Leptospira interrogans serotype 1ai strain 56601 proceeds via a threonine-independent pathway. J. Bacteriol. 186 (2004) 5400-5409. [PMID: 15292141]

[EC 2.3.1.182 created 2007]

EC 2.3.1.183

Accepted name: phosphinothricin acetyltransferase

Reaction: acetyl-CoA + phosphinothricin = CoA + N-acetylphosphinothricin

Glossary: phosphinothricin = glufosinate = 2-amino-4-[hydroxy(methyl)phosphoryl]butanoate

Other name(s): PAT; PPT acetyltransferase; Pt-N-acetyltransferase; ac-Pt

Systematic name: acetyl-CoA:phosphinothricin N-acetyltransferase

Comments: The substrate phosphinothricin is used as a nonselective herbicide and is a potent inhibitor of EC 6.3.1.2, glutamate—ammonia ligase, a key enzyme of nitrogen metabolism in plants [2].

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

References:

1. Botterman, J., Gosselé, V., Thoen, C. and Lauwereys, M. Characterization of phosphinothricin acetyltransferase and C-terminal enzymatically active fusion proteins. Gene 102 (1991) 33-37. [PMID: 1864506]

2. Dröge-Laser, W., Siemeling, U., Pühler, A. and Broer, I. The metabolites of the herbicide L-phosphinothricin (glufosinate) (identification, stability, and mobility in transgenic, herbicide-resistant, and untransformed plants). Plant Physiol. 105 (1994) 159-166. [PMID: 12232195]

[EC 2.3.1.183 created 2007]

EC 2.3.1.184

Accepted name: acyl-homoserine-lactone synthase

Reaction: an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine = an [acyl-carrier protein] + S-methyl-5'-thioadenosine + N-acyl-L-homoserine lactone

For diagram click here

Other name(s): acyl-homoserine lactone synthase; acyl homoserine lactone synthase; acyl-homoserinelactone synthase; acylhomoserine lactone synthase; AHL synthase; AHS; AHSL synthase; AhyI; AinS; AinS protein; autoinducer synthase; autoinducer synthesis protein rhlI; EsaI; ExpISCC1; ExpISCC3065; LasI; LasR; LuxI; LuxI protein; LuxM; N-acyl homoserine lactone synthase; RhlI; YspI

Systematic name: acyl-[acyl-carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing)

Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes [5]. N-(3-Oxohexanoyl)-[acyl-carrier protein] and hexanoyl-[acyl-carrier protein] are the best substrates [1]. The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier protein] rather than from fatty-acid degradation through acyl-CoA [1]. S-Adenosyl-L-methionine cannot be replaced by methionine, S-adenosylhomocysteine, homoserine or homoserine lactone [1].

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

References:

1. Schaefer, A.L., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein. Proc. Natl. Acad. Sci. USA 93 (1996) 9505-9509. [PMID: 8790360]

2. Watson, W.T., Murphy, F.V., 4th, Gould, T.A., Jambeck, P., Val, D.L., Cronan, J.E., Jr., Beck von Bodman, S. and Churchill, M.E. Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1945-1949. [PMID: 11717525]

3. Chakrabarti, S. and Sowdhamini, R. Functional sites and evolutionary connections of acylhomoserine lactone synthases. Protein Eng. 16 (2003) 271-278. [PMID: 12736370]

4. Hanzelka, B.L., Parsek, M.R., Val, D.L., Dunlap, P.V., Cronan, J.E., Jr. and Greenberg, E.P. Acylhomoserine lactone synthase activity of the Vibrio fischeri AinS protein. J. Bacteriol. 181 (1999) 5766-5770. [PMID: 10482519]

5. Parsek, M.R., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. Acyl homoserine-lactone quorum-sensing signal generation. Proc. Natl. Acad. Sci. USA 96 (1999) 4360-4365. [PMID: 10200267]

6. Ulrich, R.L. Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. Appl. Environ. Microbiol. 70 (2004) 6173-6180. [PMID: 15466564]

7. Gould, T.A., Schweizer, H.P. and Churchill, M.E. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Mol. Microbiol. 53 (2004) 1135-1146. [PMID: 15306017]

8. Raychaudhuri, A., Jerga, A. and Tipton, P.A. Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas aeruginosa. Biochemistry 44 (2005) 2974-2981. [PMID: 15723540]

9. Gould, T.A., Herman, J., Krank, J., Murphy, R.C. and Churchill, M.E. Specificity of acyl-homoserine lactone synthases examined by mass spectrometry. J. Bacteriol. 188 (2006) 773-783. [PMID: 16385066]

[EC 2.3.1.184 created 2007]

EC 2.3.1.185

Accepted name: tropine acyltransferase

Reaction: an acyl-CoA + tropine = CoA + an O-acyltropine

For diagram of reaction, click here

Glossary: tropine = tropan-3α-ol = 3α-hydroxytropane

Other name(s): tropine:acyl-CoA transferase; acetyl-CoA:tropan-3-ol acyltransferase; tropine acetyltransferase; tropine tigloyltransferase; TAT

Systematic name: acyl-CoA:tropine O-acyltransferase

Comments: This enzyme exhibits absolute specificity for the endo/3α configuration found in tropine as pseudotropine (tropan-3β-ol; see EC 2.3.1.186, pseudotropine acyltransferase) is not a substrate [3]. Acts on a wide range of aliphatic acyl-CoA derivatives, with tigloyl-CoA and acetyl-CoA being the best substrates. It is probably involved in the formation of the tropane alkaloid littorine, which is a precursor of hyoscyamine [4].

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

References:

1. Robins, R.J., Bachmann, P., Robinson, T., Rhodes, M.J. and Yamada, Y. The formation of 3α- and 3β-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases. FEBS Lett. 292 (1991) 293-297. [PMID: 1959620]

2. Robins, R.J., Bachmann,P., Peerless, A.C.J. and Rabot, S. Esterification reactions in the biosynthesis of tropane alkaloids in transformed root cultures. Plant Cell, Tissue Organ Cult. 38 (1994) 241-247.

3. Boswell, H.D., Dräger, B., McLauchlan, W.R., Portsteffen, A., Robins, D.J., Robins, R.J. and Walton, N.J. Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura. Phytochemistry 52 (1999) 871-878. [PMID: 10626376]

4. Li, R., Reed, D.W., Liu, E., Nowak, J., Pelcher, L.E., Page, J.E. and Covello, P.S. Functional genomic analysis of alkaloid biosynthesis in Hyoscyamus niger reveals a cytochrome P450 involved in littorine rearrangement. Chem. Biol. 13 (2006) 513-520. [PMID: 16720272]

[EC 2.3.1.185 created 2008]

EC 2.3.1.186

Accepted name: pseudotropine acyltransferase

Reaction: an acyl-CoA + pseudotropine = CoA + an O-acylpseudotropine

For diagram of reaction, click here

Glossary: tropine = tropan-3β-ol = 3β-hydroxytropane

Other name(s): pseudotropine:acyl-CoA transferase; tigloyl-CoA:pseudotropine acyltransferase; acetyl-CoA:pseudotropine acyltransferase; pseudotropine acetyltransferase; pseudotropine tigloyltransferase; PAT

Systematic name: acyl-CoA:pseudotropine O-acyltransferase

Comments: This enzyme exhibits absolute specificity for the exo/3β configuration found in pseudotropine as tropine (tropan-3α-ol; see EC 2.3.1.185, tropine acyltransferase) and nortropine are not substrates [1]. Acts on a wide range of aliphatic acyl-CoA derivatives, including acetyl-CoA, β-methylcrotonyl-CoA and tigloyl-CoA [1].

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

References:

1. Rabot, S., Peerless, A.C.J. and Robins, R.J. Tigloyl-CoA:pseudotropine acyltransferase — an enzyme of tropane alkaloid biosynthesis. Phytochemistry 39 (1995) 315-322.

2. Robins, R.J., Bachmann, P., Robinson, T., Rhodes, M.J. and Yamada, Y. The formation of 3α- and 3β-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases. FEBS Lett. 292 (1991) 293-297. [PMID: 1959620]

3. Robins, R.J., Bachmann,P., Peerless, A.C.J. and Rabot, S. Esterification reactions in the biosynthesis of tropane alkaloids in transformed root cultures. Plant Cell, Tissue Organ Cult. 38 (1994) 241-247.

4. Boswell, H.D., Dräger, B., McLauchlan, W.R., Portsteffen, A., Robins, D.J., Robins, R.J. and Walton, N.J. Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura. Phytochemistry 52 (1999) 871-878. [PMID: 10626376]

[EC 2.3.1.186 created 2008]

EC 2.3.1.187

Accepted name: acetyl-S-ACP:malonate ACP transferase

Reaction: an acetyl-[acyl-carrier protein] + malonate = a malonyl-[acyl-carrier protein] + acetate

For diagram of reaction click here

Other name(s): acetyl-S-ACP:malonate ACP-SH transferase; acetyl-S-acyl-carrier protein:malonate acyl-carrier-protein-transferase; MdcA; MadA; ACP transferase; malonate/acetyl-CoA transferase; malonate:ACP transferase; acetyl-S-acyl carrier protein:malonate acyl carrier protein-SH transferase

Systematic name: acetyl-[acyl-carrier-protein]:malonate S-[acyl-carrier-protein]transferase

Comments: This is the first step in the catalysis of malonate decarboxylation and involves the exchange of an acetyl thioester residue bound to the activated acyl-carrier protein (ACP) subunit of the malonate decarboxylase complex for a malonyl thioester residue [2]. This enzyme forms the α subunit of the multienzyme complexes biotin-independent malonate decarboxylase (EC 4.1.1.88) and biotin-dependent malonate decarboxylase (EC 7.2.4.4). The enzyme can also use acetyl-CoA as a substrate but more slowly [4].

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

References:

1. Hilbi, H. and Dimroth, P. Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase. Arch. Microbiol. 162 (1994) 48-56. [PMID: 18251085]

2. Hoenke, S., Schmid, M. and Dimroth, P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246 (1997) 530-538. [PMID: 9208947]

3. Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem. 266 (1999) 683-690. [PMID: 10561613]

4. Chohnan, S., Akagi, K. and Takamura, Y. Functions of malonate decarboxylase subunits from Pseudomonas putida. Biosci. Biotechnol. Biochem. 67 (2003) 214-217. [PMID: 12619701]

5. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 2.3.1.187 created 2008, modified 2018]

EC 2.3.1.188

Accepted name: ω-hydroxypalmitate O-feruloyl transferase

Reaction: feruloyl-CoA + 16-hydroxypalmitate = CoA + 16-feruloyloxypalmitate

Glossary: 16-feruloyloxypalmitate = 16-{[3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy}hexadecanoate

Other name(s): hydroxycinnamoyl-CoA ω-hydroxypalmitic acid O-hydroxycinnamoyltransferase; HHT

Systematic name: feruloyl-CoA:16-hydroxypalmitate feruloyltransferase

Comments: p-Coumaroyl-CoA and sinapoyl-CoA also act as substrates. The enzyme is widely distributed in roots of higher plants.

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

References:

1. Lotfy, S., Negrel, J. and Javelle, F. Formation of feruloyloxypalmitic acid by an enzyme from wound-healing potato tuber discs. Phytochemistry 35 (1994) 1419-1424.

2. Lotfy, S. Javelle, F. and Negrel, J. Distribution of hydroxycinnamoyl-CoA ω-hydroxypalmitic acid O-hydroxycinnamoyltransferase in higher plants. Phytochemistry 40 (1995) 389-391.

3. Lotfy, S. Javelle, F. and Negrel, J. Purification and characterization of hydroxycinnamoyl-CoA ω-hydroxypalmitic acid O-hydroxycinnamoyltransferase from tobacco (Nicotiana tabacum L.) cell-suspension cultures. Planta 199 (1996) 475-480.

[EC 2.3.1.188 created 2009]

EC 2.3.1.189

Accepted name: mycothiol synthase

Reaction: desacetylmycothiol + acetyl-CoA = CoA + mycothiol

For diagram of reaction click here

Glossary: desacetylmycothiol = 1-O-[2-(L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s): MshD

Systematic name: acetyl-CoA:desacetylmycothiol O-acetyltransferase

Comments: This enzyme catalyses the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium [1]. The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs) [2]. The enzyme has been purified from Mycobacterium tuberculosis H37Rv. Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate [3].

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

References:

1. Spies, H.S. and Steenkamp, D.J. Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis. Eur. J. Biochem. 224 (1994) 203-213. [PMID: 8076641]

2. Koledin, T., Newton, G.L. and Fahey, R.C. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch. Microbiol. 178 (2002) 331-337. [PMID: 12375100]

3. Vetting, M.W., Roderick, S.L., Yu, M. and Blanchard, J.S. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci. 12 (2003) 1954-1959. [PMID: 12930994]

[EC 2.3.1.189 created 2010]

EC 2.3.1.190

Accepted name: acetoin dehydrogenase

Reaction: acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+

Other name(s): acetoin dehydrogenase complex;acetoin dehydrogenase enzyme system;AoDH ES

Systematic name: acetyl-CoA:acetoin O-acetyltransferase

Comments: Requires thiamine diphosphate. This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyses the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic. The enzyme is composed of multiple copies of three enzymatic components:acetoin oxidoreductase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3).

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

References:

1. Priefert, H., Hein, S., Kruger, N., Zeh, K., Schmidt, B. and Steinbuchel, A. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 173 (1991) 4056-4071. [PMID: 2061286]

2. Oppermann, F.B. and Steinbuchel, A. Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J. Bacteriol. 176 (1994) 469-485. [PMID: 8110297]

3. Kruger, N., Oppermann, F.B., Lorenzl, H. and Steinbuchel, A. Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. J. Bacteriol. 176 (1994) 3614-3630. [PMID: 8206840]

4. Huang, M., Oppermann, F.B. and Steinbuchel, A. Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway. FEMS Microbiol. Lett. 124 (1994) 141-150. [PMID: 7813883]

5. Huang, M., Oppermann-Sanio, F.B. and Steinbuchel, A. Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. J. Bacteriol. 181 (1999) 3837-3841. [PMID: 10368162]

[EC 2.3.1.190 created 2010]

EC 2.3.1.191

Accepted name: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

Reaction: (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine = UDP-2,3-bis[O-(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine + a holo-[acyl-carrier protein]

For diagram of reaction click here.

Glossary: myristoyl = tetradecanoyl

Other name(s): UDP-3-O-acyl-glucosamine N-acyltransferase; UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase; acyltransferase LpxD; acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase; firA (gene name); lpxD (gene name)

Systematic name: (3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine N-acetyltransferase

Comments: The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] [1]. Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available. When grown on 1% propionic acid, lipid A also contains the odd-chain fatty acids tridecanoic acid, pentadecanoic acid, hydroxytridecanoic acid, and hydroxypentadecanoic acid [5].

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

References:

1. Bartling, C.M. and Raetz, C.R. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 48 (2009) 8672-8683. [PMID: 19655786]

2. Buetow, L., Smith, T.K., Dawson, A., Fyffe, S. and Hunter, W.N. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc. Natl. Acad. Sci. USA 104 (2007) 4321-4326. [PMID: 17360522]

3. Bartling, C.M. and Raetz, C.R. Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 47 (2008) 5290-5302. [PMID: 18422345]

4. Kelly, T.M., Stachula, S.A., Raetz, C.R. and Anderson, M.S. The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. J. Biol. Chem. 268 (1993) 19866-19874. [PMID: 8366125]

5. Bainbridge, B.W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R.K. and Darveau, R.P. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190 (2008) 4549-4558. [PMID: 18456814]

[EC 2.3.1.191 created 2010]

EC 2.3.1.192

Accepted name: glycine N-phenylacetyltransferase

Reaction: phenylacetyl-CoA + glycine = CoA + phenylacetylglycine

Other name(s): arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name)

Systematic name: phenylacetyl-CoA:glycine N-phenylacetyltransferase

Comments: Not identical with EC 2.3.1.13 (glycine N-acyltransferase). This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values.

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

References:

1. Nandi, D.L., Lucas, S.V. and Webster, L.T. Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization. J. Biol. Chem. 254 (1979) 7230-7237. [PMID: 457678]

2. Kelley, M. and Vessey, D.A. The effects of ions on the conjugation of xenobiotics by the aralkyl-CoA and arylacetyl-CoA N-acyltransferases from bovine liver mitochondria. J. Biochem. Toxicol. 5 (1990) 125-135. [PMID: 2283662]

3. Vessey, D.A. and Lau, E. Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria and its homology to the aralkyl acyl-CoA:amino acid N-acyltransferase. J Biochem Mol Toxicol 12 (1998) 275-279. [PMID: 9664233]

[EC 2.3.1.192 created 2010]

EC 2.3.1.193

Accepted name: tRNAMet cytidine acetyltransferase

Reaction: [elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA + H2O = CoA + [elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate

Other name(s): YpfI; TmcA

Systematic name: acetyl-CoA: [elongator tRNAMet]-cytidine34 N4-acetyltransferase (ATP-hydrolysing)

Comments: The enzyme acetylates the wobble base cytidine34 of the CAU anticodon of elongation-specific tRNAMet. Escherichia coli TmcA strictly discriminates elongator tRNAMet from tRNAIle, which is structurally similar and has the same anticodon loop, mainly by recognizing the C27-G43 pair in the anticodon stem. The enzyme can use GTP in place of ATP for formation of N4-acetylcytidine [1].

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

References:

1. Ikeuchi, Y., Kitahara, K. and Suzuki, T. The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon. EMBO J. 27 (2008) 2194-2203. [PMID: 18668122]

2. Chimnaronk, S., Suzuki, T., Manita, T., Ikeuchi, Y., Yao, M., Suzuki, T. and Tanaka, I. RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon. EMBO J. 28 (2009) 1362-1373. [PMID: 19322199]

[EC 2.3.1.193 created 2011]

EC 2.3.1.194

Accepted name: acetoacetyl-CoA synthase

Reaction: acetyl-CoA + malonyl-CoA = acetoacetyl-CoA + CoA + CO2

Other name(s): NphT7

Systematic name: acetyl-CoA:malonyl-CoA C-acetyltransferase (decarboxylating)

Comments: The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA to be used for mevalonate production via the mevalonate pathway. Unlike the homologous EC 2.3.1.180 (β-ketoacyl-[acyl-carrier-protein] synthase III), this enzyme does not accept malonyl-[acyl-carrier-protein] as a substrate.

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

References:

1. Okamura, E., Tomita, T., Sawa, R., Nishiyama, M. and Kuzuyama, T. Unprecedented acetoacetyl-coenzyme A synthesizing enzyme of the thiolase superfamily involved in the mevalonate pathway. Proc. Natl. Acad. Sci. USA 107 (2010) 11265-11270. [PMID: 20534558]

[EC 2.3.1.194 created 2011]

EC 2.3.1.195

Accepted name: (Z)-3-hexen-1-ol acetyltransferase

Reaction: acetyl-CoA + (3Z)-hex-3-en-1-ol = CoA + (3Z)-hex-3-en-1-yl acetate

Other name(s): CHAT; At3g03480

Systematic name: acetyl-CoA:(3Z)-hex-3-en-1-ol acetyltransferase

Comments: The enzyme is resonsible for the production of (3Z)-hex-3-en-1-yl acetate, the major volatile compound released upon mechanical wounding of the leaves of Arabidopsis thaliana [1].

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

References:

1. D'Auria, J.C., Pichersky, E., Schaub, A., Hansel, A. and Gershenzon, J. Characterization of a BAHD acyltransferase responsible for producing the green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana. Plant J. 49 (2007) 194-207. [PMID: 17163881]

2. D'Auria, J.C., Chen, F. and Pichersky, E. Characterization of an acyltransferase capable of synthesizing benzylbenzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri. Plant Physiol. 130 (2002) 466-476. [PMID: 12226525]

[EC 2.3.1.195 created 2011]

EC 2.3.1.196

Accepted name: benzyl alcohol O-benzoyltransferase

Reaction: benzoyl-CoA + benzyl alcohol = CoA + benzyl benzoate

Glossary: benzyl benzoate = benzoic acid benzyl ester

Other name(s): benzoyl-CoA:benzyl alcohol benzoyltransferase; benzoyl-CoA:benzyl alcohol/phenylethanol benzoyltransferase; benzoyl-coenzyme A:benzyl alcohol benzoyltransferase; benzoyl-coenzyme A:phenylethanol benzoyltransferase

Systematic name: benzoyl-CoA:benzyl alcohol O-benzoyltransferase

Comments: The enzyme is involved in volatile benzenoid and benzoic acid biosynthesis. The enzyme from Petunia hybrida also catalyses the formation of 2-phenylethyl benzoate from benzoyl-CoA and 2-phenylethanol. The apparent catalytic efficiency of the enzyme from Petunia hybrida with benzoyl-CoA is almost 6-fold higher than with acetyl-CoA [1].

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

References:

1. Boatright, J., Negre, F., Chen, X., Kish, C.M., Wood, B., Peel, G., Orlova, I., Gang, D., Rhodes, D. and Dudareva, N. Understanding in vivo benzenoid metabolism in Petunia petal tissue. Plant Physiol. 135 (2004) 1993-2011. [PMID: 15286288]

2. D'Auria, J.C., Chen, F. and Pichersky, E. Characterization of an acyltransferase capable of synthesizing benzylbenzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri. Plant Physiol. 130 (2002) 466-476. [PMID: 12226525]

[EC 2.3.1.196 created 2011]

EC 2.3.1.197

Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose 3-N-acetyltransferase

Reaction: acetyl-CoA + dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose = CoA + dTDP-3-acetamido-3,6-dideoxy-α-D-galactopyranose

For diagram of reaction click here.

Other name(s): FdtC; dTDP-D-Fucp3N acetylase

Systematic name: acetyl-CoA:dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose 3-N-acetyltransferase

Comments: The product, dTDP-3-acetamido-3,6-dideoxy-α-D-galactose, is a component of the glycan chain of the crystalline bacterial cell surface layer protein (S-layer glycoprotein) of Aneurinibacillus thermoaerophilus.

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

References:

1. Pfoestl, A., Hofinger, A., Kosma, P. and Messner, P. Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 278 (2003) 26410-26417. [PMID: 12740380]

[EC 2.3.1.197 created 2012]

EC 2.3.1.198

Accepted name: glycerol-3-phosphate 2-O-acyltransferase

Reaction: an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 2-acyl-sn-glycerol 3-phosphate

Other name(s): sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous)

Systematic name: acyl-CoA:sn-glycerol 3-phosphate 2-O-acyltransferase

Comments: A membrane-associated enzyme required for suberin or cutin synthesis in plants. Active with a wide range of acyl-CoA substrates (C16:0-C24:0). The enzyme from some sources has much higher activity with ω-oxidized acyl-CoAs. Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols.

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

References:

1. Yang, W., Pollard, M., Li-Beisson, Y., Beisson, F., Feig, M. and Ohlrogge, J. A distinct type of glycerol-3-phosphate acyltransferase with sn-2 preference and phosphatase activity producing 2-monoacylglycerol. Proc. Natl. Acad. Sci. USA 107 (2010) 12040-12045. [PMID: 20551224]

[EC 2.3.1.198 created 2012]

EC 2.3.1.199

Accepted name: very-long-chain 3-oxoacyl-CoA synthase

Reaction: a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA

Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.

Other name(s): very-long-chain 3-ketoacyl-CoA synthase; very-long-chain β-ketoacyl-CoA synthase; condensing enzyme (ambiguous); CUT1 (gene name); CER6 (gene name); FAE1 (gene name); KCS (gene name); ELO (gene name)

Systematic name: malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)

Comments: This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase

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

References:

1. Toke, D.A. and Martin, C.E. Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 18413-18422. [PMID: 8702485]

2. Oh, C.S., Toke, D.A., Mandala, S. and Martin, C.E. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem. 272 (1997) 17376-17384. [PMID: 9211877]

3. Dittrich, F., Zajonc, D., Huhne, K., Hoja, U., Ekici, A., Greiner, E., Klein, H., Hofmann, J., Bessoule, J.J., Sperling, P. and Schweizer, E. Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants. Eur. J. Biochem. 252 (1998) 477-485. [PMID: 9546663]

4. Millar, A.A., Clemens, S., Zachgo, S., Giblin, E.M., Taylor, D.C. and Kunst, L. CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme. Plant Cell 11 (1999) 825-838. [PMID: 10330468]

5. Ghanevati, M. and Jaworski, J.G. Engineering and mechanistic studies of the Arabidopsis FAE1 β-ketoacyl-CoA synthase, FAE1 KCS. Eur. J. Biochem. 269 (2002) 3531-3539. [PMID: 12135493]

6. Blacklock, B.J. and Jaworski, J.G. Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases. Biochem. Biophys. Res. Commun. 346 (2006) 583-590. [PMID: 16765910]

7. Denic, V. and Weissman, J.S. A molecular caliper mechanism for determining very long-chain fatty acid length. Cell 130 (2007) 663-677. [PMID: 17719544]

8. Tresch, S., Heilmann, M., Christiansen, N., Looser, R. and Grossmann, K. Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases. Phytochemistry 76 (2012) 162-171. [PMID: 22284369]

[EC 2.3.1.199 created 2012]

EC 2.3.1.200

Accepted name: lipoyl amidotransferase

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

Glossary: lipoic acid = 5-[(3R)-1,2-dithiolan-3-yl]pentanoic acid

Other name(s): LipL (gene name, ambiguous)

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

Comments: In the bacterium Listeria monocytogenes the enzyme takes part in a pathway for scavenging of lipoic acid. The enzyme is bound to 2-oxo-acid dehydrogenases such as the pyruvate dehydrogenase complex, where it transfers the lipoyl moiety from lipoyl-[glycine cleavage system H] to the E2 subunits of the complexes.

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

References:

1. Christensen, Q.H., Hagar, J.A., O'Riordan, M.X. and Cronan, J.E. A complex lipoate utilization pathway in Listeria monocytogenes. J. Biol. Chem. 286 (2011) 31447-31456. [PMID: 21768091]

[EC 2.3.1.200 created 2012]


Continued with EC 2.3.1.201 - EC 2.3.1.280
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