Enzyme Nomenclature

EC 2.4.1 (continued)

Hexosyltransferases

Continued from:
EC 2.4.1.1 to EC 2.4.1.50
EC 2.4.1.51 to EC 2.4.1.100
EC 2.4.1.101 to EC 2.4.1.150
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
See separate file for EC 2.4.1.301 to EC 2.4.1.362.

Contents

EC 2.4.1.251 GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 4-β-mannosyltransferase
EC 2.4.1.252 GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase
EC 2.4.1.253 baicalein 7-O-glucuronosyltransferase
EC 2.4.1.254 cyanidin-3-O-glucoside 2-O-glucuronosyltransferase
EC 2.4.1.255 protein O-GlcNAc transferase
EC 2.4.1.256 dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase
EC 2.4.1.257 GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
EC 2.4.1.258 dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
EC 2.4.1.259 dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
EC 2.4.1.260 dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
EC 2.4.1.261 dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
EC 2.4.1.262 soyasapogenol glucuronosyltransferase
EC 2.4.1.263 abscisate β-glucosyltransferase
EC 2.4.1.264 D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronyltransferase
EC 2.4.1.265 dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
EC 2.4.1.266 glucosyl-3-phosphoglycerate synthase
EC 2.4.1.267 dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
EC 2.4.1.268 glucosylglycerate synthase
EC 2.4.1.269 mannosylglycerate synthase
EC 2.4.1.270 mannosylglucosyl-3-phosphoglycerate synthase
EC 2.4.1.271 crocetin glucosyltransferase
EC 2.4.1.272 soyasapogenol B glucuronide galactosyltransferase
EC 2.4.1.273 soyasaponin III rhamnosyltransferase
EC 2.4.1.274 glucosylceramide β-1,4-galactosyltransferase
EC 2.4.1.275 neolactotriaosylceramide β-1,4-galactosyltransferase
EC 2.4.1.276 zeaxanthin glucosyltransferase
EC 2.4.1.277 10-deoxymethynolide desosaminyltransferase
EC 2.4.1.278 3-α-mycarosylerythronolide B desosaminyl transferase
EC 2.4.1.279 nigerose phosphorylase
EC 2.4.1.280 N,N'-diacetylchitobiose phosphorylase
EC 2.4.1.281 4-O-β-D-mannosyl-D-glucose phosphorylase
EC 2.4.1.282 3-O-α-D-glucosyl-L-rhamnose phosphorylase
EC 2.4.1.283 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
EC 2.4.1.284 2-deoxystreptamine glucosyltransferase
EC 2.4.1.285 UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase
EC 2.4.1.286 chalcone 4'-O-glucosyltransferase
EC 2.4.1.287 rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase
EC 2.4.1.288 galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase
EC 2.4.1.289 N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
EC 2.4.1.290 N,N'-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase
EC 2.4.1.291 N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase
EC 2.4.1.292 GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase
EC 2.4.1.293 GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase
EC 2.4.1.294 cyanidin 3-O-galactosyltransferase
EC 2.4.1.295 anthocyanin 3-O-sambubioside 5-O-glucosyltransferase
EC 2.4.1.296 anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase
EC 2.4.1.297 anthocyanidin 3-O-glucoside 2''-O-glucosyltransferase
EC 2.4.1.298 anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
EC 2.4.1.299 cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)
EC 2.4.1.300 cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)
See the following files for:
EC 2.4.1.301 to EC 2.4.1.362

Entries

EC 2.4.1.251

Accepted name: GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 4-β-mannosyltransferase

Reaction: GDP-mannose + GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = GDP + D-Man-β-(1→4)- GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol

For diagram of reaction click here.

Other name(s): GumI

Systematic name: GDP-mannose:GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4-β-mannosyltransferase

Comments: The enzyme is involved in the biosynthesis of the exopolysaccharide xanthan.

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

References:

1. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]

2. Ielpi, L., Couso, R.O. and Dankert, M.A. Sequential assembly and polymerization of the polyprenol-linked pentasaccharide repeating unit of the xanthan polysaccharide in Xanthomonas campestris. J. Bacteriol. 175 (1993) 2490-2500. [PMID: 7683019]

3. Kim, S.Y., Kim, J.G., Lee, B.M. and Cho, J.Y. Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae. Biotechnol. Lett. 31 (2009) 265-270. [PMID: 18854951]

[EC 2.4.1.251 created 2011]

EC 2.4.1.252

Accepted name: GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase

Reaction: GDP-mannose + D-Glc-β-(1→4)-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = GDP + D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol

For diagram of reaction click here.

Other name(s): GumH; AceA; α1,3-mannosyltransferase AceA

Systematic name: GDP-mannose:D-Glc-β-(1→4)-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase

Comments: In the bacterium Gluconacetobacter xylinus (previously known as Acetobacter xylinum) the enzyme is involved in the biosynthesis of the exopolysaccharide acetan [1]. In Xanthomonas campestris the enzyme is involved in the biosynthesis of the exopolysaccharide xanthan [5].

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

References:

1. Geremia, R.A., Roux, M., Ferreiro, D.U., Dauphin-Dubois, R., Lellouch, A.C. and Ielpi, L. Expression and biochemical characterisation of recombinant AceA, a bacterial α-mannosyltransferase. Mol. Gen. Genet. 261 (1999) 933-940. [PMID: 10485283]

2. Abdian, P.L., Lellouch, A.C., Gautier, C., Ielpi, L. and Geremia, R.A. Identification of essential amino acids in the bacterial α-mannosyltransferase aceA. J. Biol. Chem. 275 (2000) 40568-40575. [PMID: 11001941]

3. Petroni, E.A. and Ielpi, L. Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase gene from Acetobacter xylinum. J. Bacteriol. 178 (1996) 4814-4821. [PMID: 8759843]

4. Lellouch, A.C., Watt, G.M., Geremia, R.A. and Flitsch, S.L. Phytanyl-pyrophosphate-linked substrate for a bacterial α-mannosyltransferase. Biochem. Biophys. Res. Commun. 272 (2000) 290-292. [PMID: 10872841]

5. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]

[EC 2.4.1.252 created 2011]

EC 2.4.1.253

Accepted name: baicalein 7-O-glucuronosyltransferase

Reaction: UDP-D-glucuronate + baicalein = UDP + baicalin

Glossary: baicalin = 5,6,7-trihydroxyflavone-7-O-β-D-glucuronate = 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl β-D-glucupyranosiduronic acid
baicalein = 5,6,7-trihydroxyflavone = 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one
wogonin = 5,7-dihydroxy-8-methoxyflavone = 5,7-dihydroxy-8-methoxy-2-phenyl-4H-chromen-4-one
scutellarein = 4,5,6,7-tetrahydroxyflavone-7-O-β-D-glucoronate = 5,6,7-trihydroxy-2-(4-hydroxyphenyl)chromen-4-one

Other name(s): UBGAT

Systematic name: UDP-D-glucuronate:5,6,7-trihydroxyflavone 7-O-glucuronosyltransferase

Comments: The enzyme is specific for UDP-D-glucuronate as a sugar donor and flavones with substitution ortho- to the 7-OH group such as baicalein (6-OH), scutellarein (6-OH) and wogonin (8-OMe).

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

References:

1. Nagashima, S., Hirotani, M. and Yoshikawa, T. Purification and characterization of UDP-glucuronate: baicalein 7-O-glucuronosyltransferase from Scutellaria baicalensis Georgi. cell suspension cultures. Phytochemistry 53 (2000) 533-538. [PMID: 10724177]

[EC 2.4.1.253 created 2011]

EC 2.4.1.254

Accepted name: cyanidin-3-O-glucoside 2''-O-glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + cyanidin 3-O-β-D-glucoside = UDP + cyanidin 3-O-(2-O-β-D-glucuronosyl)-β-D-glucoside

For diagram of reaction click here.

Other name(s): BpUGT94B1; UDP-glucuronic acid:anthocyanin glucuronosyltransferase; UDP-glucuronic acid:anthocyanidin 3-glucoside 2'-O-β-glucuronosyltransferase; BpUGAT

Systematic name: UDP-α-D-glucuronate:cyanidin-3-O-β-D-glucoside 2-O-β-D-glucuronosyltransferase

Comments: The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-D-glucuronate. Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis [1].

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

References:

1. Sawada, S., Suzuki, H., Ichimaida, F., Yamaguchi, M.A., Iwashita, T., Fukui, Y., Hemmi, H., Nishino, T. and Nakayama, T. UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers. Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis. J. Biol. Chem. 280 (2005) 899-906. [PMID: 15509561]

2. Osmani, S.A., Bak, S., Imberty, A., Olsen, C.E. and Møller, B.L. Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses. Plant Physiol. 148 (2008) 1295-1308. [PMID: 18829982]

[EC 2.4.1.254 created 2011]

EC 2.4.1.255

Accepted name: protein O-GlcNAc transferase

Reaction: (1) UDP-N-acetyl-α-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine
(2) UDP-N-acetyl-α-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine

Other name(s): O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase

Systematic name: UDP-N-α-acetyl-D-glucosamine:[protein]-3-O-N-acetyl-β-D-glucosaminyl transferase

Comments: Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.

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

References:

1. Banerjee, S., Robbins, P.W. and Samuelson, J. Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum. Glycobiology 19 (2009) 331-336. [PMID: 18948359]

2. Clarke, A.J., Hurtado-Guerrero, R., Pathak, S., Schuttelkopf, A.W., Borodkin, V., Shepherd, S.M., Ibrahim, A.F. and van Aalten, D.M. Structural insights into mechanism and specificity of O-GlcNAc transferase. EMBO J. 27 (2008) 2780-2788. [PMID: 18818698]

3. Rao, F.V., Dorfmueller, H.C., Villa, F., Allwood, M., Eggleston, I.M. and van Aalten, D.M. Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25 (2006) 1569-1578. [PMID: 16541109]

4. Haltiwanger, R.S., Blomberg, M.A. and Hart, G.W. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 9005-9013. [PMID: 1533623]

5. Lubas, W.A., Frank, D.W., Krause, M. and Hanover, J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9316-9324. [PMID: 9083068]

6. Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P. and Walker, S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 (2011) 564-567. [PMID: 21240259]

[EC 2.4.1.255 created 2011]

EC 2.4.1.256

Accepted name: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase

Reaction: dolichyl β-D-glucosyl phosphate + D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = D-Glc-α-(1→2)-D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here.

Other name(s): ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase

Systematic name: dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase

Comments: This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.

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

References:

1. Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455-462. [PMID: 9597543]

[EC 2.4.1.256 created 2011, modified 2012]

EC 2.4.1.257

Accepted name: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase

Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolicholp> For diagram of reaction click here.

Other name(s): GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase

Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-retaining)

Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].

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

References:

1. Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900-11912. [PMID: 19282279]

2. O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593-9603. [PMID: 16878994]

[EC 2.4.1.257 created 2011, modified 2012]

EC 2.4.1.258

Accepted name: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase

Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here

Other name(s): Man5GlcNAc2-PP-Dol mannosyltransferase; ALG3; dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase; Not56-like protein; Alg3 α-1,3-mannosyl transferase; Dol-P-Man:Man5GlcNAc2-PP-Dol α-1,3-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-mannosyltransferase

Systematic name: dolichyl β-D-mannosyl phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-inverting)

Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl β-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.

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

References:

1. Sharma, C.B., Knauer, R. and Lehle, L. Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. Biol. Chem. 382 (2001) 321-328. [PMID: 11308030]

2. Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267-4277. [PMID: 10660594]

[EC 2.4.1.258 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.258, modified 2012]

EC 2.4.1.259

Accepted name: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase

Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here

Other name(s): ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase

Systematic name: dolichyl β-D-mannosyl phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)

Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate.

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

References:

1. Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910-917. [PMID: 19451548]

2. Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267-4277. [PMID: 10660594]

3. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]

[EC 2.4.1.259 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.259, modified 2012]

EC 2.4.1.260

Accepted name: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase

Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here

Other name(s): ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase

Systematic name: dolichyl β-D-mannosyl phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)

Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate.

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

References:

1. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]

2. Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792-3802. [PMID: 20023196]

3. Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749-762. [PMID: 12460943]

4. Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331-2339. [PMID: 12217961]

[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012]

EC 2.4.1.261

Accepted name: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase

Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here.

Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase

Systematic name: dolichyl β-D-mannosyl phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)

Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).

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

References:

1. Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910-917. [PMID: 19451548]

2. Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156-1163. [PMID: 15987956]

[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012]

EC 2.4.1.262

Accepted name: soyasapogenol glucuronosyltransferase

Reaction: UDP-glucuronate + soyasapogenol B = UDP + soyasapogenol B 3-O-D-glucuronide

For diagram of reaction click here.

Other name(s): UGASGT

Systematic name: UDP-D-glucuronate:soyasapogenol 3-O-D-glucuronosyltransferase

Comments: Requires a divalent ion, Mg2+ better than Mn2+, better than Ca2+. Also acts on soysapogenol A and E.

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

References:

1. Kurosawa, Y., Takahara, H. and Shiraiwa, M. UDP-glucuronic acid:soyasapogenol glucuronosyltransferase involved in saponin biosynthesis in germinating soybean seeds. Planta 215 (2002) 620-629. [PMID: 12172845]

[EC 2.4.1.262 created 2011]

EC 2.4.1.263

Accepted name: abscisate β-glucosyltransferase

Reaction: UDP-D-glucose + abscisate = UDP + β-D-glucopyranosyl abscisate

For diagram of reaction click here.

Other name(s): ABA-glucosyltransferase; ABA-GTase; AOG

Systematic name: UDP-D-glucose:abscisate β-D-glucosyltransferase

Comments: The enzyme acts better on (S)-2-trans-abscisate than the natural (S)-2-cis isomer, abscisate, or its enantiomer, the (R)-2-cis isomer.

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

References:

1. Xu, Z.J., Nakajima, M., Suzuki, Y. and Yamaguchi, I. Cloning and characterization of the abscisic acid-specific glucosyltransferase gene from adzuki bean seedlings. Plant Physiol. 129 (2002) 1285-1295. [PMID: 12114582]

[EC 2.4.1.263 created 2011]

EC 2.4.1.264

Accepted name: D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-GlcA-(1→2)-α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol

For diagram of reaction click here

Other name(s): GumK; UDP-glucuronate:D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol β-1,2-glucuronyltransferase; D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphosphoundecaprenol 2-β-glucuronyltransferase

Systematic name: UDP-α-D-glucuronate:α-D-Man-(1→3)-β-D-Glc-(1→4)-α-D-Glc-1-diphospho-ditrans,octacis-undecaprenol β-1,2-glucuronosyltransferase (configuration-inverting)

Comments: The enzyme is involved in the biosynthesis of the exopolysaccharides xanthan (in the bacterium Xanthomonas campestris) and acetan (in the bacterium Gluconacetobacter xylinus).

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

References:

1. Katzen, F., Ferreiro, D.U., Oddo, C.G., Ielmini, M.V., Becker, A., Puhler, A. and Ielpi, L. Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence. J. Bacteriol. 180 (1998) 1607-1617. [PMID: 9537354]

2. Ielpi, L., Couso, R.O. and Dankert, M.A. Sequential assembly and polymerization of the polyprenol-linked pentasaccharide repeating unit of the xanthan polysaccharide in Xanthomonas campestris. J. Bacteriol. 175 (1993) 2490-2500. [PMID: 7683019]

3. Kim, S.Y., Kim, J.G., Lee, B.M. and Cho, J.Y. Mutational analysis of the gum gene cluster required for xanthan biosynthesis in Xanthomonas oryzae pv oryzae. Biotechnol. Lett. 31 (2009) 265-270. [PMID: 18854951]

4. Barreras, M., Bianchet, M.A. and Ielpi, L. Crystallization and preliminary crystallographic characterization of GumK, a membrane-associated glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 880-883. [PMID: 16946469]

5. Barreras, M., Salinas, S.R., Abdian, P.L., Kampel, M.A. and Ielpi, L. Structure and mechanism of GumK, a membrane-associated glucuronosyltransferase. J. Biol. Chem. 283 (2008) 25027-25035. [PMID: 18596046]

6. Vojnov, A.A., Bassi, D.E., Daniels, M.J. and Dankert, M.A. Biosynthesis of a substituted cellulose from a mutant strain of Xanthomonas campestris. Carbohydr. Res. 337 (2002) 315-326. [PMID: 11841812]

7. Barreras, M., Abdian, P.L. and Ielpi, L. Functional characterization of GumK, a membrane-associated β-glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesis. Glycobiology 14 (2004) 233-241. [PMID: 14736729]

[EC 2.4.1.264 created 2011, modified 2016]

EC 2.4.1.265

Accepted name: dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase

Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here

Other name(s): ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase

Systematic name: dolichyl β-D-glucosyl phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)

Comments: The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.

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

References:

1. Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977-5981. [PMID: 8016100]

2. Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582-15590. [PMID: 3536907]

3. Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962-9971. [PMID: 12480927]

[EC 2.4.1.265 created 2011, modified 2012]

EC 2.4.1.266

Accepted name: glucosyl-3-phosphoglycerate synthase

Reaction: NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate

Other name(s): GpgS protein; GPG synthase; glucosylphosphoglycerate synthase

Systematic name: NDP-glucose:3-phospho-D-glycerate 2-α-D-glucosyltransferase

Comments: The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].

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

References:

1. Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648-1654. [PMID: 17189358]

2. Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022-1030. [PMID: 16428406]

3. Empadinhas, N., Albuquerque, L., Mendes, V., Macedo-Ribeiro, S. and da Costa, M.S. Identification of the mycobacterial glucosyl-3-phosphoglycerate synthase. FEMS Microbiol. Lett. 280 (2008) 195-202. [PMID: 18221489]

4. Pereira, P.J., Empadinhas, N., Albuquerque, L., Sa-Moura, B., da Costa, M.S. and Macedo-Ribeiro, S. Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis. PLoS One 3 (2008) e3748. [PMID: 19015727]

5. Gest, P., Kaur, D., Pham, H.T., van der Woerd, M., Hansen, E., Brennan, P.J., Jackson, M. and Guerin, M.E. Preliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis in Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1121-1124. [PMID: 19052364]

6. Kaur, D., Pham, H., Larrouy-Maumus, G., Riviere, M., Vissa, V., Guerin, M.E., Puzo, G., Brennan, P.J. and Jackson, M. Initiation of methylglucose lipopolysaccharide biosynthesis in mycobacteria. PLoS One 4 (2009) e544. [PMID: 19421329]

[EC 2.4.1.266 created 2011]

EC 2.4.1.267

Accepted name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase

Reaction: dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate

For diagram of reaction click here

Other name(s): ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase

Systematic name: dolichyl β-D-glucosyl phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)

Comments: The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.

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

References:

1. Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493-498. [PMID: 8877369]

2. Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412-417. [PMID: 6423630]

3. Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420-421. [PMID: 14517965]

[EC 2.4.1.267 created 2011, modified 2012]

EC 2.4.1.268

Accepted name: glucosylglycerate synthase

Reaction: ADP-glucose + D-glycerate = 2-O-(α-D-glucopyranosyl)-D-glycerate + ADP

Other name(s): Ggs (gene name)

Systematic name: ADP-glucose:D-glycerate 2-α-D-glucosyltransferase

Comments: Persephonella marina possesses two enzymatic systems for the synthesis of glucosylglycerate. The first one is a single-step pathway in which glucosylglycerate synthase catalyses the synthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate. The second system is a two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of NDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 (glucosyl-3-phosphoglycerate phosphatase).

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

References:

1. Fernandes, C., Empadinhas, N. and da Costa, M.S. Single-step pathway for synthesis of glucosylglycerate in Persephonella marina. J. Bacteriol. 189 (2007) 4014-4019. [PMID: 17369297]

2. Fernandes, C., Mendes, V., Costa, J., Empadinhas, N., Jorge, C., Lamosa, P., Santos, H. and da Costa, M.S. Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis. J. Bacteriol. 192 (2010) 1624-1633. [PMID: 20061481]

[EC 2.4.1.268 created 2011]

EC 2.4.1.269

Accepted name: mannosylglycerate synthase

Reaction: GDP-α-D-mannose + D-glycerate = GDP + 2-O-(α-D-mannopyranosyl)-D-glycerate

Systematic name: GDP-α-D-mannose:D-glycerate 2-α-D-mannosyltransferase

Comments: Rhodothermus marinus can also form mannosylglycerate via a two-step pathway catalysed by EC 2.4.1.217 (mannosyl-3-phosphoglycerate synthase) and EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase) [1]. Depending on experimental conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate [1,2].

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

References:

1. Martins, L.O., Empadinhas, N., Marugg, J.D., Miguel, C., Ferreira, C., da Costa, M.S. and Santos, H. Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase. J. Biol. Chem. 274 (1999) 35407-35414. [PMID: 10585410]

2. Flint, J., Taylor, E., Yang, M., Bolam, D.N., Tailford, L.E., Martinez-Fleites, C., Dodson, E.J., Davis, B.G., Gilbert, H.J. and Davies, G.J. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat. Struct. Mol. Biol. 12 (2005) 608-614. [PMID: 15951819]

[EC 2.4.1.269 created 2011]

EC 2.4.1.270

Accepted name: mannosylglucosyl-3-phosphoglycerate synthase

Reaction: GDP-mannose + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate = GDP + 2-O-[2-O-(α-D-mannopyranosyl)-α-D-glucopyranosyl]-3-phospho-D-glycerate

Other name(s): MggA

Systematic name: GDP-mannose:2-O-(α-D-glucosyl)-3-phospho-D-glycerate 2-O-α-D-mannosyltransferase

Comments: The enzyme is involved in synthesis of 2-[2-O-(α-D-mannopranosyl)-α-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.

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

References:

1. Fernandes, C., Mendes, V., Costa, J., Empadinhas, N., Jorge, C., Lamosa, P., Santos, H. and da Costa, M.S. Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis. J. Bacteriol. 192 (2010) 1624-1633. [PMID: 20061481]

[EC 2.4.1.270 created 2011]

EC 2.4.1.271

Accepted name: crocetin glucosyltransferase

Reaction: (1) UDP-α-D-glucose + crocetin = UDP + β-D-glucosyl crocetin
(2) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + bis(β-D-glucosyl) crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin

For diagram of reaction click here.

Other name(s): crocetin GTase; UGTCs2; UGT75L6; UDP-glucose:crocetin glucosyltransferase; UDP-glucose:crocetin 8-O-D-glucosyltransferase

Systematic name: UDP-α-D-glucose:crocetin 8-O-D-glucosyltransferase

Comments: In the plants Crocus sativus and Gardenia jasminoides this enzyme esterifies a free carboxyl group of crocetin and some crocetin glycosyl esters. The enzyme from Gardenia can also form glucosyl esters with 4-coumarate, caffeate and ferulate [3].

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

References:

1. Côté, F., Cormier, F., Dufresne, C. and Willemot, C. Properties of a glucosyltransferase involved in crocin synthesis. Plant Sci. 153 (2000) 55-63.

2. Moraga, A.R., Nohales, P.F., Perez, J.A. and Gomez-Gomez, L. Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta 219 (2004) 955-966. [PMID: 15605174]

3. Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett 586 (2012) 1055-1061. [PMID: 22569263]

[EC 2.4.1.271 created 2011]

EC 2.4.1.272

Accepted name: soyasapogenol B glucuronide galactosyltransferase

Reaction: UDP-α-D-galactose + soyasapogenol B 3-O-β-D-glucuronide = UDP + soyasaponin III

For diagram of reaction click here.

Glossary: soyasaponin III = 3β-(2-O-β-D-galactopyranosyl-β-D-glucopyranosyloxyuronic acid)olean-12-ene-22β,24-diol

Other name(s): UDP-galactose:SBMG-galactosyltransferase; UGT73P2; GmSGT2 (gene name); UDP-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase

Systematic name: UDP-α-D-galactose:soyasapogenol B 3-O-glucuronide β-D-galactosyltransferase

Comments: Part of the biosynthetic pathway for soyasaponins.

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

References:

1. Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258-2264. [PMID: 20350545]

[EC 2.4.1.272 created 2011]

EC 2.4.1.273

Accepted name: soyasaponin III rhamnosyltransferase

Reaction: UDP-β-L-rhamnose + soyasaponin III = UDP + soyasaponin I

For diagram of reaction click here.

Glossary: UDP-β-L-rhamnose = UDP-6-deoxy-β-L-mannose

Other name(s): UGT91H4; GmSGT3 (gene name); UDP-rhamnose:soyasaponin III rhamnosyltransferase

Systematic name: UDP-β-L-rhamnose:soyasaponin III rhamnosyltransferase

Comments: Part of the biosynthetic pathway for soyasaponins.

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

References:

1. Shibuya, M., Nishimura, K., Yasuyama, N. and Ebizuka, Y. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584 (2010) 2258-2264. [PMID: 20350545]

[EC 2.4.1.273 created 2011]

EC 2.4.1.274

Accepted name: glucosylceramide β-1,4-galactosyltransferase

Reaction: UDP-α-D-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Other name(s): lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading); UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase

Systematic name: UDP-α-D-galactose:β-D-glucosyl-(1↔1)-ceramide 4-β-galactosyltransferase

Comments: Involved in the synthesis of several different major classes of glycosphingolipids.

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

References:

1. Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136-142. [PMID: 3099851]

2. Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719-2724. [PMID: 1900430]

3. Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148-7153. [PMID: 1551920]

4. Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570-13577. [PMID: 9593693]

5. Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301-304. [PMID: 10320813]

[EC 2.4.1.274 created 2011]

EC 2.4.1.275

Accepted name: neolactotriaosylceramide β-1,4-galactosyltransferase

Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide

Other name(s): β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect)

Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase

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

References:

1. Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331-29340. [PMID: 9792633]

[EC 2.4.1.275 created 2011, modified 2013]

EC 2.4.1.276

Accepted name: zeaxanthin glucosyltransferase

Reaction: 2 UDP-glucose + zeaxanthin = 2 UDP + zeaxanthin bis(β-D-glucoside)

For diagram of reaction, click here

Other name(s): crtX (gene name)

Systematic name: UDP-glucose:zeaxanthin β-D-glucosyltransferase

Comments: The reaction proceeds in two steps with the monoglucoside as an intermediate.

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

References:

1. Hundle, B.S., O'Brien, D.A., Alberti, M., Beyer, P. and Hearst, J.E. Functional expression of zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site. Proc. Natl. Acad. Sci. USA 89 (1992) 9321-9325. [PMID: 1409639]

[EC 2.4.1.276 created 2011]

EC 2.4.1.277

Accepted name: 10-deoxymethynolide desosaminyltransferase

Reaction: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin

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

Glossary: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose = dTDP-D-desosamine

Other name(s): glycosyltransferase DesVII; DesVII

Systematic name: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase

Comments: DesVII is the glycosyltransferase responsible for the attachment of dTDP-D-desosamine to 10-deoxymethynolide or narbonolide during the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in the bacterium Streptomyces venezuelae. Activity requires an additional protein partner, DesVIII.

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

References:

1. Borisova, S.A. and Liu, H.W. Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway. Biochemistry 49 (2010) 8071-8084. [PMID: 20695498]

2. Borisova, S.A., Kim, H.J., Pu, X. and Liu, H.W. Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications. Chembiochem. 9 (2008) 1554-1558. [PMID: 18548476]

3. Hong, J.S., Park, S.J., Parajuli, N., Park, S.R., Koh, H.S., Jung, W.S., Choi, C.Y. and Yoon, Y.J. Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation. Gene 386 (2007) 123-130. [PMID: 17049185]

[EC 2.4.1.277 created 2011, modified 2014]

EC 2.4.1.278

Accepted name: 3-α-mycarosylerythronolide B desosaminyl transferase

Reaction: dTDP-D-desosamine + 3-α-L-mycarosylerythronolide B = dTDP + erythromycin D

For diagram of reaction click here.

Glossary: dTDP-D-desosamine = dTDP-3,4,6-trideoxy-3-(dimethylamino)-α-D-xylo-hexopyranose
erythromycin D = (3R,4S,5S,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-7,12-dihydroxy-6-[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyloxy]-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione
3-O-α-mycarosylerythronolide B = (3R,4S,5R,6R,7R,9R,11R,12S,13R,14R)-4-(2,6-dideoxy-3-C-methyl-α-L-ribo-hexopyranosyloxy)-14-ethyl-6,7,12-trihydroxy-3,5,7,9,11,13-hexamethyloxacyclotetradecane-2,10-dione

Other name(s): EryCIII; dTDP-3-dimethylamino-4,6-dideoxy-α-D-glucopyranose:3-α-mycarosylerythronolide B 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase; desosaminyl transferase EryCIII

Systematic name: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose:3-α-mycarosylerythronolide B 3-dimethylamino-3,4,6-trideoxy-β-D-glucosyltransferase

Comments: The enzyme is involved in erythromycin biosynthesis.

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

References:

1. Yuan, Y., Chung, H.S., Leimkuhler, C., Walsh, C.T., Kahne, D. and Walker, S. In vitro reconstitution of EryCIII activity for the preparation of unnatural macrolides. J. Am. Chem. Soc. 127 (2005) 14128-14129. [PMID: 16218575]

2. Lee, H.Y., Chung, H.S., Hang, C., Khosla, C., Walsh, C.T., Kahne, D. and Walker, S. Reconstitution and characterization of a new desosaminyl transferase, EryCIII, from the erythromycin biosynthetic pathway. J. Am. Chem. Soc. 126 (2004) 9924-9925. [PMID: 15303858]

3. Moncrieffe, M.C., Fernandez, M.J., Spiteller, D., Matsumura, H., Gay, N.J., Luisi, B.F. and Leadlay, P.F. Structure of the glycosyltransferase EryCIII in complex with its activating P450 homologue EryCII. J. Mol. Biol. 415 (2012) 92-101. [PMID: 22056329]

[EC 2.4.1.278 created 2012, modified 2014]

EC 2.4.1.279

Accepted name: nigerose phosphorylase

Reaction: 3-O-α-D-glucopyranosyl-D-glucopyranose + phosphate = D-glucose + β-D-glucose 1-phosphate

Glossary: 3-O-α-D-glucopyranosyl-D-glucopyranose = nigerose

Other name(s): cphy1874 (gene name)

Systematic name: 3-O-α-D-glucopyranosyl-D-glucopyranose:phosphate β-D-glucosyltransferase

Comments: The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230, kojibiose phosphorylase)

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

References:

1. Nihira, T., Nakai, H., Chiku, K. and Kitaoka, M. Discovery of nigerose phosphorylase from Clostridium phytofermentans. Appl. Microbiol. Biotechnol. 93 (2012) 1513-1522. [PMID: 21808968]

[EC 2.4.1.279 created 2012]

EC 2.4.1.280

Accepted name: N,N'-diacetylchitobiose phosphorylase

Reaction: N,N'-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-α-D-glucosamine 1-phosphate

Glossary: N,N'-diacetylchitobiose = N-acetyl-D-glucosaminyl-β-(1→4)-N-acetyl-D-glucosamine

Other name(s): chbP (gene name)

Systematic name: N,N'-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase

Comments: The enzyme is specific for N,N'-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.

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

References:

1. Park, J.K., Keyhani, N.O. and Roseman, S. Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N'-diacetylchitobiose phosphorylase. J. Biol. Chem. 275 (2000) 33077-33083. [PMID: 10913116]

2. Honda, Y., Kitaoka, M. and Hayashi, K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem. J. 377 (2004) 225-232. [PMID: 13678418]

3. Hidaka, M., Honda, Y., Kitaoka, M., Nirasawa, S., Hayashi, K., Wakagi, T., Shoun, H. and Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold. Structure 12 (2004) 937-947. [PMID: 15274915]

[EC 2.4.1.280 created 2012]

EC 2.4.1.281

Accepted name: 4-O-β-D-mannosyl-D-glucose phosphorylase

Reaction: 4-O-β-D-mannopyranosyl-D-glucopyranose + phosphate = D-glucose + α-D-mannose 1-phosphate

Glossary: 4-O-β-D-mannopyranosyl-D-glucopyranose = β-D-mannopyranosyl-(1→4)-D-glucopyranose

Other name(s): mannosylglucose phosphorylase

Systematic name: 4-O-β-D-mannopyranosyl-D-glucopyranose:phosphate α-D-mannosyltransferase

Comments: This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.

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

References:

1. Senoura, T., Ito, S., Taguchi, H., Higa, M., Hamada, S., Matsui, H., Ozawa, T., Jin, S., Watanabe, J., Wasaki, J. and Ito, S. New microbial mannan catabolic pathway that involves a novel mannosylglucose phosphorylase. Biochem. Biophys. Res. Commun. 408 (2011) 701-706. [PMID: 21539815]

[EC 2.4.1.281 created 2012]

EC 2.4.1.282

Accepted name: 3-O-α-D-glucosyl-L-rhamnose phosphorylase

Reaction: 3-O-α-D-glucopyranosyl-L-rhamnopyranose + phosphate = L-rhamnopyranose + β-D-glucose 1-phosphate

Other name(s): cphy1019 (gene name)

Systematic name: 3-O-α-D-glucopyranosyl-L-rhamnopyranose:phosphate β-D-glucosyltransferase

Comments: The enzyme does not phosphorylate α,α-trehalose, kojibiose, nigerose, or maltose. In the reverse phosphorolysis reaction the enzyme is specific for L-rhamnose as acceptor and β-D-glucose 1-phosphate as donor.

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

References:

1. Nihira, T., Nakai, H. and Kitaoka, M. 3-O-α-D-Glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans. Carbohydr. Res. 350 (2012) 94-97. [PMID: 22277537]

[EC 2.4.1.282 created 2012]

EC 2.4.1.283

Accepted name: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + 2-deoxystreptamine = UDP + 2'-N-acetylparomamine

For diagram of reaction click here.

Other name(s): btrM (gene name); neoD (gene name); kanF (gene name)

Systematic name: UDP-N-acetyl-α-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase

Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-α-D-glucosamine [1].

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

References:

1. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]

2. Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843-852. [PMID: 21983602]

[EC 2.4.1.283 created 2012]

EC 2.4.1.284

Accepted name: 2-deoxystreptamine glucosyltransferase

Reaction: UDP-α-D-glucose + 2-deoxystreptamine = UDP + 2'-deamino-2'-hydroxyparomamine

Glossary: 2'-deamino-2'-hydroxyparomamine = 4-O-α-D-glucopyranosyl-2-deoxy-D-streptamine

Other name(s): kanF (gene name)

Systematic name: UDP-α-D-glucose:2-deoxystreptamine 6-α-D-glucosyltransferase

Comments: Involved in the biosynthesis of kanamycin B and kanamycin C. Also catalyses EC 2.4.1.283, 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase, but activity is only one fifth of that with UDP-α-D-glucose.

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

References:

1. Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843-852. [PMID: 21983602]

[EC 2.4.1.284 created 2012]

EC 2.4.1.285

Accepted name: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + ribostamycin = UDP + 2′′′-acetyl-6′′′-hydroxyneomycin C

Other name(s): neoK (gene name)

Systematic name: UDP-N-acetyl-α-D-glucosamine:ribostamycin N-acetylglucosaminyltransferase

Comments: Involved in biosynthesis of the aminoglycoside antibiotic neomycin. Requires a divalent metal ion, optimally Mg2+, Mn2+ or Co2+.

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

References:

1. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]

[EC 2.4.1.285 created 2012]

EC 2.4.1.286

Accepted name: chalcone 4'-O-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + 2',4,4',6'-tetrahydroxychalcone = UDP + 2',4,4',6'-tetrahydroxychalcone 4'-O-β-D-glucoside
(2) UDP-α-D-glucose + 2',3,4,4',6'-pentahydroxychalcone = UDP + 2',3,4,4',6'-pentahydroxychalcone 4'-O-β-D-glucoside

For diagram of reaction click here.

Glossary: 2',4,4',6'-tetrahydroxychalcone = 3-(4-hydroxyphemyl)-1-(2,4,6-trihydroxyphenyl)prop-2-en-1-one

Other name(s): 4’CGT

Systematic name: UDP-α-D-glucose:2',4,4',6'-tetrahydroxychalcone 4'-O-β-D-glucosyltransferase

Comments: Isolated from the plant Antirrhinum majus (snapdragon). Involved in the biosynthesis of aurones, plant flavonoids that provide yellow color to the flowers.

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

References:

1. Ono, E., Fukuchi-Mizutani, M., Nakamura, N., Fukui, Y., Yonekura-Sakakibara, K., Yamaguchi, M., Nakayama, T., Tanaka, T., Kusumi, T. and Tanaka, Y. Yellow flowers generated by expression of the aurone biosynthetic pathway. Proc. Natl. Acad. Sci. USA 103 (2006) 11075-11080. [PMID: 16832053]

[EC 2.4.1.286 created 2012]

EC 2.4.1.287

Accepted name: rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase

Reaction: 2 UDP-α-D-galactofuranose + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = 2 UDP + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol (overall reaction)
(1a) UDP-α-D-galactofuranose + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol = UDP + β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol
(1b) UDP-α-D-galactofuranose + β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol = UDP + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans-octacis-decaprenol

For diagram of reaction click here.

Other name(s): arabinogalactan galactofuranosyl transferase 1; GlfT1

Systematic name: UDP-α-D-galactofuranose:α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-β/4-β-galactofuranosyltransferase (configuration-inverting)

Comments: Isolated from the bacteria Mycobacterium tuberculosis and M. smegmatis, the enzyme has dual β-(1→4) and β-(1→5) transferase action. Involved in the formation of the cell wall in mycobacteria.

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

References:

1. Mikusová, K., Belánová, M., Korduláková, J., Honda, K., McNeil, M.R., Mahapatra, S., Crick, D.C. and Brennan, P.J. Identification of a novel galactosyl transferase involved in biosynthesis of the mycobacterial cell wall. J. Bacteriol. 188 (2006) 6592-6598. [PMID: 16952951]

2. Belánová, M., Dianisková, P., Brennan, P.J., Completo, G.C., Rose, N.L., Lowary, T.L. and Mikusová, K. Galactosyl transferases in mycobacterial cell wall synthesis. J. Bacteriol. 190 (2008) 1141-1145. [PMID: 18055597]

[EC 2.4.1.287 created 2012, modified 2017]

EC 2.4.1.288

Accepted name: galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase

Reaction: 28 UDP-α-D-galactofuranose + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = 28 UDP + [β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→6)]14-β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol

For diagram of reaction click here.

Other name(s): GlfT2

Systematic name: UDP-α-D-galactofuranose:β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-β/5-β-D-galactofuranosyltransferase

Comments: Isolated from Mycobacterium tuberculosis. The enzyme adds approximately twenty-eight galactofuranosyl residues with alternating 1→5 and 1→6 links forming a galactan domain with approximately thirty galactofuranosyl residues. Involved in the formation of the cell wall in mycobacteria.

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

References:

1. Rose, N.L., Zheng, R.B., Pearcey, J., Zhou, R., Completo, G.C. and Lowary, T.L. Development of a coupled spectrophotometric assay for GlfT2, a bifunctional mycobacterial galactofuranosyltransferase. Carbohydr. Res. 343 (2008) 2130-2139. [PMID: 18423586]

2. May, J.F., Splain, R.A., Brotschi, C. and Kiessling, L.L. A tethering mechanism for length control in a processive carbohydrate polymerization. Proc. Natl. Acad. Sci. USA 106 (2009) 11851-11856. [PMID: 19571009]

3. Wheatley, R.W., Zheng, R.B., Richards, M.R., Lowary, T.L. and Ng, K.K. Tetrameric structure of GlfT2 reveals a scaffold for the assembly of mycobacterial arabinogalactan. J. Biol. Chem. (2012) . [PMID: 22707726]

[EC 2.4.1.288 created 2012]

EC 2.4.1.289

Accepted name: N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase

Reaction: dTDP-6-deoxy-β-L-mannose + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = dTDP + α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol

For diagram of reaction click here.

Glossary: dTDP-6-deoxy-β-L-mannose = dTDP-4-β-L-rhamnose

Other name(s): WbbL

Systematic name: dTDP-6-deoxy-β-L-mannose:N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-α-L-rhamnosyltransferase

Comments: Requires Mn2+ or Mg2+. Isolated from Mycobacterium smegmatis [1] and Mycobacterium tuberculosis [2]. The enzyme catalyses the addition of a rhamnosyl unit to N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol, completing the synthesis of the linkage unit that attaches the arabinogalactan moiety to the peptidoglycan moiety in Mycobacterial cell wall.

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

References:

1. Mills, J.A., Motichka, K., Jucker, M., Wu, H.P., Uhlik, B.C., Stern, R.J., Scherman, M.S., Vissa, V.D., Pan, F., Kundu, M., Ma, Y.F. and McNeil, M. Inactivation of the mycobacterial rhamnosyltransferase, which is needed for the formation of the arabinogalactan-peptidoglycan linker, leads to irreversible loss of viability. J. Biol. Chem. 279 (2004) 43540-43546. [PMID: 15294902]

2. Grzegorzewicz, A.E., Ma, Y., Jones, V., Crick, D., Liav, A. and McNeil, M.R. Development of a microtitre plate-based assay for lipid-linked glycosyltransferase products using the mycobacterial cell wall rhamnosyltransferase WbbL. Microbiology 154 (2008) 3724-3730. [PMID: 19047740]

[EC 2.4.1.289 created 2012]

EC 2.4.1.290

Accepted name: N,N'-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→3)-N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol

For diagram of reaction click here.

Glossary: N,N'-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose

Other name(s): PglA

Systematic name: UDP-N-acetyl-α-D-galactosamine:N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase

Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

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

References:

1. Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255-14259. [PMID: 16186480]

[EC 2.4.1.290 created 2012]

EC 2.4.1.291

Accepted name: N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-D-galactosaminyl-α-(1→3)-N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→4)-N-acetyl-D-galactosaminyl-α-(1→3)-N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol

For diagram of reaction click here.

Glossary: N,N'-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose

Other name(s): PglJ

Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetylgalactosaminyl-α-(1→3)-N,N'-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase

Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

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

References:

1. Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255-14259. [PMID: 16186480]

2. Chen, M.M., Weerapana, E., Ciepichal, E., Stupak, J., Reid, C.W., Swiezewska, E. and Imperiali, B. Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 46 (2007) 14342-14348. [PMID: 18034500]

[EC 2.4.1.291 created 2012]

EC 2.4.1.292

Accepted name: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase

Reaction: 3 UDP-N-acetyl-α-D-galactosamine + GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol = 3 UDP + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol

For diagram of reaction click here.

Glossary: diNAcBac = N,N'-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose

Other name(s): PglH

Systematic name: UDP-N-acetyl-α-D-galactosamine:GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-α-N-acetyl-D-galactosaminyltransferase

Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

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

References:

1. Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255-14259. [PMID: 16186480]

2. Troutman, J.M. and Imperiali, B. Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. Biochemistry 48 (2009) 2807-2816. [PMID: 19159314]

3. Borud, B., Viburiene, R., Hartley, M.D., Paulsen, B.S., Egge-Jacobsen, W., Imperiali, B. and Koomey, M. Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system. Proc. Natl. Acad. Sci. USA 108 (2011) 9643-9648. [PMID: 21606362]

[EC 2.4.1.292 created 2012]

EC 2.4.1.293

Accepted name: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase

Reaction: UDP-α-D-glucose + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol = UDP + [GalNAc-α-(1→4)]2-[Glc-β-(1→3)]-[GalNAc-α-(1→4)]2-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol

For diagram of reaction click here.

Glossary: diNAcBac = N,N'-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose

Other name(s): PglI

Systematic name: UDP-α-D-glucose:[GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-β-D-glucosyltransferase

Comments: Isolated from the bacterium Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

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

References:

1. Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255-14259. [PMID: 16186480]

2. Kelly, J., Jarrell, H., Millar, L., Tessier, L., Fiori, L.M., Lau, P.C., Allan, B. and Szymanski, C.M. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J. Bacteriol. 188 (2006) 2427-2434. [PMID: 16547029]

[EC 2.4.1.293 created 2012]

EC 2.4.1.294

Accepted name: cyanidin 3-O-galactosyltransferase

Reaction: UDP-α-D-galactose + cyanidin = UDP + cyanidin 3-O-β-D-galactoside

For diagram of reaction click here.

Glossary: cyanidin = 3,3',4',5,7-pentahydroxyflavylium

Other name(s): UDP-galactose:cyanidin galactosyltransferase

Systematic name: UDP-α-D-galactose:cyanidin 3-O-galactosyltransferase

Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).

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

References:

1. Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397-403. [PMID: 8717136]

[EC 2.4.1.294 created 2013]

EC 2.4.1.295

Accepted name: anthocyanin 3-O-sambubioside 5-O-glucosyltransferase

Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-sambubioside = UDP + an anthocyanidin 5-O-β-D-glucoside 3-O-β-D-sambubioside

For diagram of reaction click here.

Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)

Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-β-D-sambubioside 5-O-glucosyltransferase

Comments: Isolated from the plant Matthiola incana (stock). No activity with anthocyanidin 3-O-glucosides.

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

References:

1. Teusch, M., Forkmann, G. and Seyffert, W. Genetic control of UDP-glucose: anthocyanin 5-O-glucosyltransferase from flowers of Matthiola incana R.Br. Planta 168 (1986) 586-591.

[EC 2.4.1.295 created 2013]

EC 2.4.1.296

Accepted name: anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase

Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] = UDP + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucoside

For diagram of reaction click here.

Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-[3-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucosyltransferase

Comments: Isolated from the plant Petunia hybrida. It does not act on an anthocyanidin 3-O-rutinoside

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

References:

1. Jonsson, L.M.V., Aarsman, M.E.G., van Diepen, J., de Vlaming, P., Smit, N. and Schram, A.W. Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida. Planta 160 (1984) 341-347.

[EC 2.4.1.296 created 2013]

EC 2.4.1.297

Accepted name: anthocyanidin 3-O-glucoside 2''-O-glucosyltransferase

Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-sophoroside

For diagram of reaction click here.

Glossary: anthocyanidin 3-O-sophoroside = anthocyanidin 3-O-(β-D-glucosyl(1→2)-β-D-glucoside)

Other name(s): 3GGT

Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-glucoside 2''-O-glucosyltransferase

Comments: Isolated from Ipomoea nil (Japanese morning glory).

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

References:

1. Morita, Y., Hoshino, A., Kikuchi, Y., Okuhara, H., Ono, E., Tanaka, Y., Fukui, Y., Saito, N., Nitasaka, E., Noguchi, H. and Iida, S. Japanese morning glory dusky mutants displaying reddish-brown or purplish-gray flowers are deficient in a novel glycosylation enzyme for anthocyanin biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2''-O-glucosyltransferase, due to 4-bp insertions in the gene. Plant J. 42 (2005) 353-363. [PMID: 15842621]

[EC 2.4.1.297 created 2013]

EC 2.4.1.298

Accepted name: anthocyanidin 3-O-glucoside 5-O-glucosyltransferase

Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3,5-di-O-β-D-glucoside

For diagram of reaction click here.

Other name(s): UDP-glucose:anthocyanin 5-O-glucosyltransferase

Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-β-D-glucoside 5-O-glucosyltransferase

Comments: Isolated from the plants Perilla frutescens var. crispa, Verbena hybrida [1], Dahlia variabilis [2] and Gentiana triflora (clustered gentian) [3]. It will also act on anthocyanidin 3-O-(6-O-malonylglucoside) [2] and is much less active with hydroxycinnamoylglucose derivatives [3]. There is no activity in the absence of the 3-O-glucoside group.

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

References:

1. Yamazaki, M., Gong, Z., Fukuchi-Mizutani, M., Fukui, Y., Tanaka, Y., Kusumi, T. and Saito, K. Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin. J. Biol. Chem. 274 (1999) 7405-7411. [PMID: 10066805]

2. Ogata, J., Sakamoto, T., Yamaguchi, M., Kawanobu, S., Yoshitama, K. Isolation and characterization of anthocyanin 5-O-glucosyltransferase from flowers of Dahlia variabilis. J. Plant Physiol. 158 (2001) 709-714.

3. Nakatsuka, T., Sato, K., Takahashi, H., Yamamura, S. and Nishihara, M. Cloning and characterization of the UDP-glucose:anthocyanin 5-O-glucosyltransferase gene from blue-flowered gentian. J. Exp. Bot. 59 (2008) 1241-1252. [PMID: 18375606]

[EC 2.4.1.298 created 2013]

EC 2.4.1.299

Accepted name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

Reaction: 1-O-sinapoyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = sinapate + cyanidin 3,5-di-O-β-D-glucoside

For diagram of reaction click here.

Glossary: sinapate = 4-hydroxy-3,5-dimethoxycinnamate
cyanidin = 3,3',4',5,7-pentahydroxyflavylium

Other name(s): AA5GT

Systematic name: 1-O-sinapoyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 5-O-β-D-glucosyltransferase

Comments: Isolated from the plant Dianthus caryophyllus (carnation). Also acts on other anthocyanidins and with other acyl-glucose donors. cf. EC 2.4.1.298, anthocyanidin 3-O-glucoside 5-O-glucosyltransferase.

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

References:

1. Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374-3389. [PMID: 20971893]

2. Nishizaki, Y., Matsuba, Y., Okamoto, E., Okamura, M., Ozeki, Y. and Sasaki, N. Structure of the acyl-glucose-dependent anthocyanin 5-O-glucosyltransferase gene in carnations and its disruption by transposable elements in some varieties. Mol. Genet. Genomics 286 (2011) 383-394. [PMID: 22048706]

[EC 2.4.1.299 created 2013]

EC 2.4.1.300

Accepted name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

Reaction: 1-O-vanilloyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = vanillate + cyanidin 3,7-di-O-β-D-glucoside

For diagram of reaction click here.

Glossary: vanillate = 4-hydroxy-3-methoxybenzoate
cyanidin = 3,3',4',5,7-pentahydroxyflavylium

Other name(s): AA7GT

Systematic name: 1-O-vanilloyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 7-O-β-D-glucosyltransferase

Comments: Isolated from the plant Delphinium grandiflorum (delphinium). Also acts on other anthocyanidins and with other acyl-glucose derivatives.

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

References:

1. Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374-3389. [PMID: 20971893]

[EC 2.4.1.300 created 2013]


Continued with EC 2.4.1.301-EC 2.4.1.362
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