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
See separate file for EC 2.4.1.251 to EC 2.4.1.300 and EC 2.4.1.301 to EC 2.4.1.368.

Contents

EC 2.4.1.201 α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
EC 2.4.1.202 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2 -D-glucosyltransferase
EC 2.4.1.203 zeatin O-β-D-glucosyltransferase
EC 2.4.1.204 now EC 2.4.2.40
EC 2.4.1.205 galactogen 6β-galactosyltransferase
EC 2.4.1.206 lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase
EC 2.4.1.207 xyloglucan:xyloglucosyl transferase
EC 2.4.1.208 diglucosyl diacylglycerol synthase (1,2-linking)
EC 2.4.1.209 cis-p-coumarate glucosyltransferase
EC 2.4.1.210 limonoid glucosyltransferase
EC 2.4.1.211 1,3-β-galactosyl-N-acetylhexosamine phosphorylase
EC 2.4.1.212 hyaluronan synthase
EC 2.4.1.213 glucosylglycerol-phosphate synthase
EC 2.4.1.214 glycoprotein 3-α-L-fucosyltransferase
EC 2.4.1.215 cis-zeatin O-β-D-glucosyltransferase
EC 2.4.1.216 trehalose 6-phosphate phosphorylase
EC 2.4.1.217 mannosyl-3-phosphoglycerate synthase
EC 2.4.1.218 hydroquinone glucosyltransferase
EC 2.4.1.219 vomilenine glucosyltransferase
EC 2.4.1.220 indoxyl-UDPG glucosyltransferase
EC 2.4.1.221 peptide-O-fucosyltransferase
EC 2.4.1.222 O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase
EC 2.4.1.223 glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
EC 2.4.1.224 glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
EC 2.4.1.225 N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase
EC 2.4.1.226 N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase
EC 2.4.1.227 undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase
EC 2.4.1.228 lactosylceramide 4-α-galactosyltransferase
EC 2.4.1.229 [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
EC 2.4.1.230 kojibiose phosphorylase
EC 2.4.1.231 α,α-trehalose phosphorylase (configuration-retaining)
EC 2.4.1.232 glycolipid 6-α-mannosyltransferase
EC 2.4.1.233 deleted now EC 2.4.1.115
EC 2.4.1.234 kaempferol 3-O-galactosyltransferase
EC 2.4.1.235 cyanidin 3-O-rutinoside 5-O-glucosyltransferase
EC 2.4.1.235 now *EC 2.4.1.116
EC 2.4.1.236 flavanone 7-O-glucoside 2"-O-β-L-rhamnosyltransferase
EC 2.4.1.237 flavonol 7-O-β-glucosyltransferase
EC 2.4.1.238 delphinidin 3,5-di-O-glucoside 3'-O-glucosyltransferase
EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase
EC 2.4.1.240 flavonol-3-O-glycoside glucosyltransferase
EC 2.4.1.241 digalactosyldiacylglycerol synthase
EC 2.4.1.242 NDP-glucose—starch glucosyltransferase
EC 2.4.1.243 6G-fructosyltransferase
EC 2.4.1.244 N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase
EC 2.4.1.245 α,α-trehalose synthase
EC 2.4.1.246 mannosylfructose-phosphate synthase
EC 2.4.1.247 β-D-galactosyl-(1→4)-L-rhamnose phosphorylase
EC 2.4.1.248 cycloisomaltooligosaccharide glucanotransferase
EC 2.4.1.249 delphinidin 3',5'-O-glucosyltransferase
EC 2.4.1.250 D-inositol-3-phosphate glycosyltransferase

See the following file for:
EC 2.4.1.251 to EC 2.4.1.300
EC 2.4.1.301 to EC 2.4.1.368

Entries

EC 2.4.1.201

Accepted name: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]

For diagram of reaction click here.

Other name(s): MGAT4C (gene name); N-acetylglucosaminyltransferase VI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI; uridine diphosphoacetylglucosamine-glycopeptide β-1→4-acetylglucosaminyltransferase VI; mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTVI; GlcNAc-T VI; UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→2)]-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)

Comments: Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in β1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by β linkages. No homologous enzyme appears to exist in mammals.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119699-68-2

References:

1. Brockhausen, I., Hull, E., Hindsgaul, O., Schachter, H., Shah, R.N., Michnick, S.W. and Carver, J.P. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc β1-6 (GlcNAc β1-2)Man α-R (GlcNAc to Man) β-4-N-acetylglucosaminyltransferase VI. J. Biol. Chem. 264 (1989) 11211-11221. [PMID: 2525556]

2. Taguchi, T., Ogawa, T., Inoue, S., Inoue, Y., Sakamoto, Y., Korekane, H. and Taniguchi, N. Purification and characterization of UDP-GlcNAc:GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man]-β1,4-N-acetylglucosaminyltransferase VI from hen oviduct. J. Biol. Chem. 275 (2000) 32598-32602. [PMID: 10903319]

3. Sakamoto, Y., Taguchi, T., Honke, K., Korekane, H., Watanabe, H., Tano, Y., Dohmae, N., Takio, K., Horii, A. and Taniguchi, N. Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcβ 1-6(GlcNAcβ 1-2)- manα 1-R[GlcNAc to man]β 1,4N-acetylglucosaminyltransferase VI. J. Biol. Chem. 275 (2000) 36029-36034. [PMID: 10962001]

[EC 2.4.1.201 created 1992, modified 2001, modified 2018]

EC 2.4.1.202

Accepted name: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase

Reaction: (1) UDP-α-D-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
(2) UDP-α-D-glucose + 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside

For diagram of reaction click here.

Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = DIMBOA
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIMBOA β-D-glucoside

Other name(s): uridine diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-glucosyltransferase; BX8; BX9; benzoxazinoid glucosyltransferase; DIMBOA glucosyltransferase

Systematic name: UDP-α-D-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-β-D-glucosyltransferase

Comments: The enzyme is involved in the detoxification of the benzoxazinoids DIBOA (2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one) and DIMBOA (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) which are stored as the respective non-toxic glucosides in the vacuoles in some plants, most commonly from the family of Poaceae (grasses). Benzoxazinoids are known to exhibit antimicrobial, antifeedant, and antiinsecticidal effects and are involved in the interaction of plants with other plants, insects, or microorganisms.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122544-56-3

References:

1. Bailey, B.A. and Larson, R.L. Hydroxamic acid glucosyltransferases from maize seedlings. Plant Physiol. 90 (1989) 1071-1076. [PMID: 16666853]

2. von Rad, U., Huttl, R., Lottspeich, F., Gierl, A. and Frey, M. Two glucosyltransferases are involved in detoxification of benzoxazinoids in maize. Plant J. 28 (2001) 633-642. [PMID: 11851909]

[EC 2.4.1.202 created 1992, modified 2012]

EC 2.4.1.203

Accepted name: trans-zeatin O-β-D-glucosyltransferase

Reaction: UDP-glucose + trans-zeatin = UDP + O-β-D-glucosyl-trans-zeatin

Glossary:
zeatin

Other name(s): zeatin O-β-D-glucosyltransferase; uridine diphosphoglucose-zeatin O-glucosyltransferase; zeatin O-glucosyltransferase

Systematic name: UDP-glucose:trans-zeatin O-β-D-glucosyltransferase

Comments: Unlike EC 2.4.1.215, cis-zeatin O-β-D-glucosyltransferase, UDP-D-xylose can also act as donor (cf. EC 2.4.2.40, zeatin O-β-D-xylosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123644-76-8

References:

1. Dixon, S.C., Martin, R.C., Mok, R.C., Shaw, G. and Mok, D.W.S. Zeatin glycosylation enzymes in Phaseolus - isolation of O-glucosyltransferase from Phaseolus lunatus and comparison to O-xylosyltransferase from P. vulgaris. Plant Physiol. 90 (1989) 1316-1321.

[EC 2.4.1.203 created 1992, modified 2001]

[EC 2.4.1.204 Transferred entry: now EC 2.4.2.40, zeatin O-β-D-xylosyltransferase (EC 2.4.1.204 created 1992, deleted 2003)]

EC 2.4.1.205

Accepted name: galactogen 6β-galactosyltransferase

Reaction: UDP-galactose + galactogen = UDP + (1→6)-β-D-galactosylgalactogen

Other name(s): uridine diphosphogalactose-galactogen galactosyltransferase; 1,6-D-galactosyltransferase; β-(1-6)-D-galactosyltransferase

Systematic name: UDP-galactose:galactogen β-1,6-D-galactosyltransferase

Comments: Galactogen from Helix pomatia is the most effective acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 88273-54-5

References:

1. Goudsmit, E.M., Ketchum, P.A., Grossens, M.K. and Blake, D.A. Biosynthesis of galactogen: identification of a β-(1→6)-D-galactosyltransferase in Helix pomatia albumen glands. Biochim. Biophys. Acta 992 (1989) 289-297. [PMID: 2505854]

[EC 2.4.1.205 created 1992]

EC 2.4.1.206

Accepted name: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + 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: GlcA = glucuronic acid

Other name(s): spHAS; seHAS; Alternating UDP-α-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase

Systematic name: Alternating UDP-N-acetyl-α-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase (configuration-inverting)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83682-80-8

References:

1. Gottfries, J., Percy, A.K., Månsson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253-261. [PMID: 1825612]

2. Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1--3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649-15658. [PMID: 2960671]

3. Percy, A.K., Gottfries, J., Vilbergsson, G., Månsson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461-1465. [PMID: 1901591]

[EC 2.4.1.206 created 1992]

EC 2.4.1.207

Accepted name: xyloglucan:xyloglucosyl transferase

Reaction: breaks a β-(1→4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan

Other name(s): endo-xyloglucan transferase; xyloglucan endotransglycosylase

Systematic name: xyloglucan:xyloglucan xyloglucanotransferase

Comments: does not use cello-oligosaccharides as either donor or acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 141588-40-1

References:

1. Fry, S.C., Smith, R.C., Renwick, K.F., Hodge, S.C., Matthews, K.J. Xyloglucan endotransglycosylase, a new cell wall-loosening activity from plants. Biochem. J. 282 (1992) 821-828. [PMID: 1554366]

2. Nishitani, K., Tominaga, R. Endoxyloglucan transferase, a novel class of glucosyltransferase that catalyzes transfer of a segment of xyloglucan to another xyloglucan molecule. J. Biol. Chem. 267 (1992) 21058-21064. [PMID: 1400418]

3. De Silva, J., Jarman, C.D., Arrowsmith, D.A., Stronach, M.S., Chengappa, S., Sidebottom, C., Reid, J.S.G. Molecular characterisation of a xyloglucan-specific endo-(1→4)-β-D-glucanase (xyloglucan endotransglucosylase) from nasturtium seeds. Plant J. 3 (1993) 701-711. [PMID: 8374619]

4. Lorences, E.P., Fry, S.C. Xyloglucan oligosaccharides with at least two α-D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan. Plant Physiol. 88 (1993) 105-112.

[EC 2.4.1.207 created 1999]

EC 2.4.1.208

Accepted name: diglucosyl diacylglycerol synthase (1,2-linking)

Reaction: UDP-α-D-glucose + 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[α-D-glucopyranosyl-(1→2)-O-α-D-glucopyranosyl]-sn-glycerol + UDP

Other name(s): monoglucosyl diacylglycerol (1→2) glucosyltransferase; MGlcDAG (1→2) glucosyltransferase; DGlcDAG synthase (ambiguous); UDP-glucose:1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol (1→2) glucosyltransferase; diglucosyl diacylglycerol synthase

Systematic name: UDP-α-D-glucose:1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol 2-glucosyltransferase

Comments: The enzyme from Acholeplasma laidlawii requires Mg2+.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 168680-19-1

References:

1. Karlsson, O.P., Rytomaa, M., Dahlqvist, A., Kinnunen, P.K., Wieslander, A. Correlation between bilayer lipid dynamics and activity of the diglucosyldiacylglycerol synthase from Acholeplasma laidlawii membranes. Biochemistry 35 (1996) 10094-10102. [PMID: 8756472]

[EC 2.4.1.208 created 1999, modified 2014]

EC 2.4.1.209

Accepted name: cis-p-coumarate glucosyltransferase

Reaction: UDP-glucose + cis-p-coumarate = 4'-O-β-D-glucosyl-cis-p-coumarate + UDP

Systematic name: UDP-glucose:cis-p-coumarate β-D-glucosyltransferase

Comments: cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 196887-88-4

References:

1. Rasmussen, S. and Rudolph, H. Isolation, purification and characterization of UDP-glucose:cis-p-coumaric acid-β-D-glucosyltransferase from Sphagnum fallax. Phytochemistry 46 (1997) 449-453.

[EC 2.4.1.209 created 2000]

EC 2.4.1.210

Accepted name: limonoid glucosyltransferase

Reaction: UDP-glucose + limonin = glucosyl-limonin + UDP

Other name(s): uridine diphosphoglucose-limonoid glucosyltransferase

Systematic name: UDP-glucose:limonin glucosyltransferase

Comments: The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 195836-82-9

References:

1. Shin, H., Suhayda, C.G., Hsu, W.-J. and Robertson, G.H. Purification of limonoid glucosyltransferase from navel orange albedo tissue. Phytochemistry 46 (1997) 33-37.

[EC 2.4.1.210 created 2000]

EC 2.4.1.211

Accepted name: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

Reaction: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine + phosphate = α-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine

Other name(s): lacto-N-biose phosphorylase; LNBP; galacto-N-biose phosphorylase

Systematic name: β-D-galactopyranosyl-(1→3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase

Comments: Reaction also occurs with β-D-galactopyranosyl-(1→3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 224427-06-9

References:

1. Derensy-Dron, D., Krzewinski, F., Brassart, C. and Bouquelet S. β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation. Biotechnol. Appl. Biochem. 29 (1999) 3-10. [PMID: 9889079]

[EC 2.4.1.211 created 2001]

EC 2.4.1.212

Accepted name: hyaluronan synthase

Reaction: (1) UDP-α-N-acetyl-D-glucosamine + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan]
(2) UDP-α-D-glucuronate + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan] = UDP + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan]

For diagram click here.

Glossary: GlcNAc = N-acetyl-D-glucosamine
GlcA = glucuronic acid

Other name(s): spHAS; seHAS

Systematic name: Alternating UDP-α-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase

Comments: The enzyme from Streptococcus Group A and Group C requires Mg2+. The enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc [3]. The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in a variety of organisms.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39346-43-5

References:

1. DeAngelis, P.L., Papaconstantinou, J. and Weigel, P.H. Molecular cloning, identification and sequence of the hyaluronan synthase gene from Group A Streptococcus pyogenes. J. Biol. Chem. 268 (1993) 19181-19184. [PMID: 8366070]

2. Jing, W. and DeAngelis, P.L. Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. Glycobiology 10 (2000) 883-889. [PMID: 10988250]

3. DeAngelis, P.L. Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 274 (1999) 26557-26562. [PMID: 10473619]

4. Tlapak-Simmons, V.L., Baron, C.A. and Weigel, P.H. Characterization of the purified hyaluronan synthase from Streptococcus equisimilis. Biochemistry 43 (2004) 9234;9242. [PMID: 15248781]

[EC 2.4.1.212 created 2001, modified 2007]

EC 2.4.1.213

Accepted name: glucosylglycerol-phosphate synthase

Reaction: ADP-α-D-glucose + sn-glycerol 3-phosphate = 2-(α-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP

Other name(s): ADP-glucose:sn-glycerol-3-phosphate 2-β-D-glucosyltransferase (incorrect)

Systematic name: ADP-α-D-glucose:sn-glycerol-3-phosphate 2-α-D-glucopyranosyltransferase

Comments: Acts with EC 3.1.3.69 (glucosylglycerol phosphatase) to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 161515-13-5

References:

1. Hagemann, M. and Erdmann, N. Activation and pathway of glucosylglycerol biosynthesis in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology 140 (1994) 1427-1431.

2. Marin, K., Zuther, E., Kerstan, T., Kunert, A. and Hagemann, M. The ggpS gene from Synechocystis sp. strain PCC 6803 encoding glucosylglycerol-phosphate synthase is involved in osmolyte synthesis. J. Bacteriol. 180 (1998) 4843-4849. [PMID: 9733686]

[EC 2.4.1.213 created 2001, modified 2015]

EC 2.4.1.214

Accepted name: glycoprotein 3-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-[α-L-fucosyl-(1→3)]-N-acetyl-β-D-glucosaminyl}asparagine

For diagram click here.

Other name(s): GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc)-Asn-peptide) α1→3-fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase

Systematic name: GDP-β-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 3-α-L-fucosyl-transferase

Comments: Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-α-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-β-L-fucose to form an α1,3-linkage rather than an α1,6-linkage. The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68247-53-0

References:

1. Wilson, I.B.H., Rendic, D., Freilinger, A., Dumic, J., Altmann, F., Mucha, J., Müller, S. and Hauser, M.-T. Cloning and expression of α1,3-fucosyltransferase homologues from Arabidopsis thaliana. Biochim. Biophys. Acta 1527 (2001) 88-96. [PMID: 11420147]

2. Fabini, G., Freilinger, A., Altmann, F. and Wilson, I.B.H. Identification of core α1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J. Biol. Chem. 276 (2001) 28058-28067. [PMID: 11382750]

3. Leiter, H., Mucha, J., Staudacher, E., Grimm, R., Glössl, J. and Altmann, F. Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase from mung beans. J. Biol. Chem. 274 (1999) 21830-21839. [PMID: 10419500]

4. van Tetering, A., Schiphorst, W.E.C.M., van den Eijnden, D.H. and van Die, I. Characterization of core α1→3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex type N-glycans. FEBS Lett. 461 (1999) 311-314. [PMID: 10567717]

5. Staudacher, E., Altmann, F., Glössl, J., März, L., Schachter, H., Kamerling, J.P., Hård, K. and Vliegenthart, J.F.G. GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc)-Asn-peptide) α1→3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem. 199 (1991) 745-751. [PMID: 1868856]

[EC 2.4.1.214 created 2001]

EC 2.4.1.215

Accepted name: cis-zeatin O-β-D-glucosyltransferase

Reaction: UDP-glucose + cis-zeatin = UDP + O-β-D-glucosyl-cis-zeatin

Glossary:
zeatin

Systematic name: UDP-glucose:cis-zeatin O-β-D-glucosyltransferase

Comments: The enzyme from maize can use cis-zeatin and UDP-glucose as substrates, but not cis-ribosylzeatin, trans-zeatin or trans-ribosylzeatin. Unlike EC 2.4.1.203, trans-zeatin O-β-D-glucosyltransferase, UDP-D-xylose cannot act as a donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123644-76-8

References:

1. Martin, R.C., Mok, M.C., Habben, J.E. and Mok, D.W.S. A maize cytokinin gene encoding an O-glucosyltransferase specific to cis-zeatin. Proc. Natl. Acad. Sci. USA 98 (2001) 5922-5926. [PMID: 11331778]

[EC 2.4.1.215 created 2001]

EC 2.4.1.216

Accepted name: trehalose 6-phosphate phosphorylase

Reaction: α,α-trehalose 6-phosphate + phosphate = glucose 6-phosphate + β-D-glucose 1-phosphate

Systematic name: α,α-trehalose 6-phosphate:phosphate β-D-glucosyltransferase

Comments: The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate. Differs from EC 2.4.1.64, α,α-trehalose phosphorylase, in that trehalose is not a substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 403512-51-6

References:

1. Andersson, U., Levander, F. and Radstrom, P. Trehalose 6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. J. Biol. Chem. 276 (2001) 42707-42713. [PMID: 11553642]

[EC 2.4.1.216 created 2001]

EC 2.4.1.217

Accepted name: mannosyl-3-phosphoglycerate synthase

Reaction: GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(α-D-mannosyl)-3-phosphoglycerate

Other name(s): MPG synthase; GDP-mannose:3-phosphoglycerate 3-α-D-mannosyltransferase

Systematic name: GDP-mannose:3-phospho-D-glycerate 3-α-D-mannosyltransferase

Comments: Requires Mg2+. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 393512-63-5

References:

1. Empadinhas, N., Marugg, J.D., Borges, N., Santos, H. and da Costa, M.S. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key-enzymes. J. Biol. Chem. 276 (2001) 43580-43588. [PMID: 11562374]

[EC 2.4.1.217 created 2002]

EC 2.4.1.218

Accepted name: hydroquinone glucosyltransferase

Reaction: UDP-glucose + hydroquinone = UDP + hydroquinone-O-β-D-glucopyranoside

Other name(s): arbutin synthase; hydroquinone:O-glucosyltransferase

Systematic name: UDP-glucose:hydroquinone-O-β-D-glucosyltransferase

Comments: Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates.

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

References:

1. Arend, J., Warzecha, H. and Stöckigt, J. Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences. Phytochemistry 53 (2000) 187-193. [PMID: 10680170]

2. Arend, J., Warzecha, H., Hefner, T. and Stöckigt, J. Utilizing genetically engineered bacteria to produce plant specific glucosides. Biotechnol. Bioeng. 76 (2001) 126-131. [PMID: 11505382]

[EC 2.4.1.218 created 2002]

EC 2.4.1.219

Accepted name: vomilenine glucosyltransferase

Reaction: UDP-glucose + vomilenine = UDP + raucaffricine

For diagram click here.

Other name(s): UDPG:vomilenine 21-β-D-glucosyltransferase

Systematic name: UDP-glucose:vomilenine 21-O-β-D-glucosyltransferase

Comments: The indole alkaloid raucaffricine accumulates during the culture of Rauvolfia cell suspensions.

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

References:

1. Warzecha, H., Obitz, P. and Stöckigt, J. Purification, partial amino acid sequence and structure of the product of raucaffricine-O-β-D-glucosidase from plant cell cultures of Rauwolfia serpentina. Phytochemistry 50 (1999) 1099-1109. [PMID: 10234858]

2. Warzecha, H., Gerasimenko, I., Kutchan, T.M. and Stöckigt, J. Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis. Phytochemistry 54 (2000) 657-666. [PMID: 10975500]

3. Ruyter, C.M., and Stöckigt, J. Enzymatic formation of raucaffricine, the major indole alkaloid of Rauwolfia serpentina cell-suspension cultures. Helv. Chim. Acta 74 (1991) 1707-1712.

[EC 2.4.1.219 created 2002]

EC 2.4.1.220

Accepted name: indoxyl-UDPG glucosyltransferase

Reaction: UDP-glucose + indoxyl = UDP + indican

Glossary: indoxyl = indole-3-ol

Other name(s): indoxyl-UDPG-glucosyltransferase

Systematic name: UDP-glucose:indoxyl 3-O-β-D-glucosyltransferase

Comments: Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole. After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 258339-72-9

References:

1. Marcinek, H., Weyler, W., Deus-Neumann, B. and Zenk, M.H. Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia. Phytochemistry 53 (2000) 201-207. [PMID: 10680172]

[EC 2.4.1.220 created 2002]

EC 2.4.1.221

Accepted name: peptide-O-fucosyltransferase

Reaction: transfers an α-L-fucosyl residue from GDP-β-L-fucose to the serine hydroxy group of a protein acceptor

Other name(s): GDP-L-fucose:polypeptide fucosyltransferase; GDP-fucose protein O-fucosyltransferase; GDP-fucose:polypeptide fucosyltransferase

Systematic name: GDP-β-L-fucose:polypeptide O-α-L-fucosyltransferase

Comments: Involved in the biosynthesis of O-fucosylated epidermal growth factor (EGF) and thrombospondin type 1 repeats. The attachment of O-linked fucose to serine or threonine occurs on EGF domains within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-08-3

References:

1. Wang, Y. and Spellman, M.W. Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells. J. Biol. Chem. 273 (1998) 8112-8118. [PMID: 9525914]

2. Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P. and Haltiwanger, R.S. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. J. Biol. Chem. 276 (2001) 40338-40345. [PMID: 11524432]

3. Wang, Y., Lee, G.F., Kelley, R.F. and Spellman, M.W. Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains. Glycobiology 6 (1996) 837-842. [PMID: 9023546]

4. Hofsteenge, J., Huwiler, K.G., Macek, B., Hess, D., Lawler, J., Mosher, D.F. and Peter-Katalinic, J. C-mannosylation and O-fucosylation of the thrombospondin type 1 module. J. Biol. Chem. 276 (2001) 6485-6498. [PMID: 11067851]

[EC 2.4.1.221 created 2002]

EC 2.4.1.222

Accepted name: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase

Reaction: transfers a β-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor

Other name(s): O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase; fringe

Systematic name: UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase

Comments: O-Fucosylpeptide 3-β-N-acetylglucosaminyltransferases are the products of fringe genes. O-linked fucose is an unusual form of glycosylation where the fucose is attached directly to proteins through the hydroxy groups of Ser or Thr residues.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 299203-70-6

References:

1. Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369-375. [PMID: ] 10935626]

[EC 2.4.1.222 created 2002]

EC 2.4.1.223

Accepted name: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(α-D-GlcNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine

For diagram of reaction click here.

Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine

Other name(s): α-N-acetylglucosaminyltransferase I; α1,4-N-acetylglucosaminyltransferase; glucuronosylgalactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl-proteoglycan 4IV-α-N-acetyl-D-glucosaminyltransferase; glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4IV-α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)

Comments: Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. Apparently products of both the human EXTL2 and EXTL3 genes can catalyse this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. For explanation of the use of a superscript in the systematic name, see 2-Carb-37.2.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 179241-74-8

References:

1. Kitagawa, H., Shimakawa, H. and Sugahara, K. The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274 (1999) 13933-13937. [PMID: 10318803]

2. Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834-4838. [PMID: 11121397]

[EC 2.4.1.223 created 2002, modified 2016]

EC 2.4.1.224

Accepted name: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan = UDP + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan

For diagram click here.

Other name(s): α-N-acetylglucosaminyltransferase II glucuronyl-N-acetylglucosaminylproteoglycan α-1,4-N-acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase

Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the 4-β-glucuronosyltransferase (EC 2.4.1.225, N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase) activity required for the synthesis of the heparan sulfate disaccharide repeats. Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-α-N-acetylglucosaminyltransferase activity. In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223, glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 336193-98-7

References:

1. Kim, B.T., Kitagawa, H., Tamura, J., Saito, T., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode α1,4-N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/heparin biosynthesis. Proc. Natl. Acad. Sci. USA 98 (2001) 7176-7181. [PMID: 11390981]

2. Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834-4838. [PMID: 11121397]

3. Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282-286. [PMID: 11256613]

4. Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265-26268. [PMID: 9756849]

[EC 2.4.1.224 created 2002]

EC 2.4.1.225

Accepted name: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase

Reaction: UDP-α-D-glucuronate + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan = UDP + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan

For diagram click here.

Other name(s): N-acetylglucosaminylproteoglycan β-1,4-glucuronyltransferase; heparan glucuronyltransferase II

Systematic name: UDP-α-D-glucuronate:N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 4-β-glucuronosyltransferase

Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 145539-84-0

References:

1. Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282-286. [PMID: 11256613]

2. Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265-26268. [PMID: 9756849]

[EC 2.4.1.225 created 2002]

EC 2.4.1.226

Accepted name: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase

Reaction: (1) UDP-α-D-glucuronate + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
(2) UDP-α-D-glucuronate + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine

For diagram of reaction click here.

Other name(s): chondroitin glucuronyltransferase II; α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase; UDP-α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase

Systematic name: UDP-α-D-glucuronate:[protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 3-β-glucuronosyltransferase (configuration-inverting)

Comments: Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 269077-98-7

References:

1. Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721-38726. [PMID: 11514575]

2. DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124-24129. [PMID: 10818104]

3. Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567-21575. [PMID: 11943778]

4. Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine. J. Biol. Chem. 277 (2002) 38179-38188. [PMID: 12145278]

[EC 2.4.1.226 created 2002, modified 2018]

EC 2.4.1.227

Accepted name: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

For diagram of reaction click here.

Other name(s): MurG transferase; UDP-N-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase (configuration-inverting)

Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 60976-26-3

References:

1. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]

[EC 2.4.1.227 created 2002]

EC 2.4.1.228

Accepted name: lactosylceramide 4-α-galactosyltransferase

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

For diagram of reaction click here.

Glossary: lactosylceramide = β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide

Other name(s): Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose; UDP-galactose:lactosylceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl(1↔1)ceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase

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

Comments: For explanation of superscript II in systematic name, see 2-carb.37.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52725-57-2

References:

1. Bailly, P., Piller, F., Cartron, J.P., Leroy, Y. and Fournet, B. Identification of UDP-galactose: lactose (lactosylceramide) α-4 and β-3 galactosyltransferases in human kidney. Biochem. Biophys. Res. Commun. 141 (1986) 84-91. [PMID: 3099784]

2. Steffensen, R., Carlier, K., Wiels, J., Levery, S.B., Stroud, M., Cedergren, B., Nilsson Sojka, B., Bennett, E.P., Jersild, C. and Clausen, H. Cloning and expression of the histo-blood group Pk UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype. J. Biol. Chem. 275 (2000) 16723-16729. [PMID: 10747952]

3. Kojima, Y., Fukumoto, S., Furukawa, K., Okajima, T., Wiels, J., Yokoyama, K., Suzuki, Y., Urano, T., Ohta, M. and Furukawa, K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152-15156. [PMID: 10748143]

[EC 2.4.1.228 created 2002]

EC 2.4.1.229

Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase

Reaction: UDP-N-acetylglucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-D-glucosaminyl)-trans-4-hydroxy-L-proline

Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase

Systematic name: UDP-N-acetyl-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-D-glucosaminyl-transferase

Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 256531-81-4

References:

1. van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328-46337. [PMID: 12244115]

2. Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392-36402. [PMID: 10593934]

3. West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [PMID: 11886837]

[EC 2.4.1.229 created 2003, modified 2013]

EC 2.4.1.230

Accepted name: kojibiose phosphorylase

Reaction: 2-α-D-glucosyl-D-glucose + phosphate = D-glucose + β-D-glucose 1-phosphate

For diagram click here.

Systematic name: 2-α-D-glucosyl-D-glucose:phosphate β-D-glucosyltransferase

Comments: The enzyme from Thermoanaerobacter brockii can act with α-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. The enzyme is inactive when dissaccharides with linkages other than α-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 206566-36-1

References:

1. Chaen, H., Yamamoto, T., Nishimoto, T., Nakada, T., Fukuda, S., Sugimoto, T., Kurimoto, M. and Tsujisaka, Y. Purification and characterization of a novel phosphorylase, kojibiose phosphorylase, from Thermoanaerobium brockii. J. Appl. Glycosci. 46 (1999) 423-429.

2. Chaen, H., Nishimoto, T., Nakada, T., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Enzymatic synthesis of kojioligosaccharides using kojibiose phosphorylase. J. Biosci. Bioeng. 92 (2001) 177-182.

[EC 2.4.1.230 created 2003]

EC 2.4.1.231

Accepted name: α,α-trehalose phosphorylase (configuration-retaining)

Reaction: α,α-trehalose + phosphate = α-D-glucose + α-D-glucose 1-phosphate

For diagram of reaction click here

Other name(s): trehalose phosphorylase[ambiguous]

Systematic name: α,α-trehalose:phosphate α-D-glucosyltransferase

Comments: Unlike EC 2.4.1.64, α,α-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.

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

References:

1. Eis, C. and Nidetzky, B. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. Biochem. J. 363 (2002) 335-340. [PMID: 11931662]

2. Eis, C., Watkins, M., Prohaska, T. and Nidetzky, B. Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem. J. 356 (2001) 757-767. [PMID: 11389683]

3. Nidetzky, B. and Eis, C. α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem. J. 360 (2001) 727-736. [PMID: 11736665]

[EC 2.4.1.231 created 2003]

EC 2.4.1.232

Accepted name: initiation-specific α-1,6-mannosyltransferase

Reaction: Transfers an α-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an α-(1→6)-D-mannosyl-D-mannose linkage

Other name(s): α-1,6-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase; GDP-mannose:glycolipid 1,6-α-D-mannosyltransferase; glycolipid 6-α-mannosyltransferase

Systematic name: GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase

Comments: Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 346003-17-6

References:

1. Romero, P.A. and Herscovics, A. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of α-1,6-mannosyltransferase which initiates outer chain formation. J. Biol. Chem. 264 (1989) 1946-1950. [PMID: 2644248]

2. Reason, A.J., Dell, A., Romero, P.A. and Herscovics, A. Specificity of the mannosyltransferase which initiates outer chain formation in Saccharomyces cerevisiae. Glycobiology 1 (1991) 387-391. [PMID: 1820199]

3. Nakanishi-Shindo, Y., Nakayama, K., Tanaka, A., Toda, Y. and Jigami, Y. Structure of the N-linked oligosaccharides that show the complete loss of α-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 26338-26345. [PMID: 8253757]

4. Yamamoto, K., Okamoto, M., Yoko-o, T. and Jigami, Y. Salt stress induces the expression of the Schizosaccharomyces pombe och1+, which encodes an initiation-specific α-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins. Biosci. Biotechnol. Biochem. 67 (2003) 927-929. [PMID: 12784644]

5. Cui, Z., Horecka, J. and Jigami, Y. Cdc4 is involved in the transcriptional control of OCH1, a gene encoding α-1,6-mannosyltransferase in Saccharomyces cerevisiae. Yeast 19 (2002) 69-77. [PMID: 11754484]

6. Tsukahara, K., Watanabe, T., Yoko-o, T. and Chigami, Y. Schizosaccharomyces pombe och1+ gene encoding α-1,6-mannosyltransferase and use of och1+ gene knockout fission yeast for production of glycoproteins with reduced glycosylation. Jpn. Kokai Tokkyo Koho (2001) 11 pp.

7. Nakayama, K., Nakanishi-Shindo, Y., Tanaka, A., Haga-Toda, Y. and Jigami, Y. Substrate specificity of α-1,6-mannosyltransferase that initiates N-linked mannose outer chain elongation in Saccharomyces cerevisiae. FEBS Lett. 412 (1997) 547-550. [PMID: 9276464]

8. Suzuki, A., Shibata, N., Suzuki, M., Saitoh, F., Takata, Y., Oshie, A., Oyamada, H., Kobayashi, H., Suzuki, S. and Okawa, Y. Characterization of α-1,6-mannosyltransferase responsible for the synthesis of branched side chains in Candida albicans mannan. Eur. J. Biochem. 240 (1996) 37-44. [PMID: 8797833]

9. Yip, C.L., Welch, S.K., Klebl, F., Gilbert, T., Seidel, P., Grant, F., O'Hara, P.J. and MacKay, V.L. Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 2723-2727. [PMID: 8146181]

[EC 2.4.1.232 created 2004]

[EC 2.4.1.233 Deleted entry: anthocyanidin 3-O-glucosyltransferase. The enzyme is identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase (EC 2.4.1.233 created 2004, deleted 2005)]

EC 2.4.1.234

Accepted name: kaempferol 3-O-galactosyltransferase

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

For diagram click here.

Other name(s): F3GalTase; UDP-galactose:kaempferol 3-O-β-D-galactosyltransferase

Systematic name: UDP-α-D-galactose:kaempferol 3-O-β-D-galactosyltransferase

Comments: Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin. The reaction can occur equally well in both directions.

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

References:

1. Miller, K.D., Guyon, V., Evans, J.N., Shuttleworth, W.A. and Taylor, L.P. Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida. J. Biol. Chem. 274 (1999) 34011-34019. [PMID: 10567367]

[EC 2.4.1.234 created 2004]

[EC 2.4.1.235 Deleted entry: Enzyme is identical to EC 2.4.1.116, cyanidin 3-O-rutinoside 5-O-glucosyltransferase (EC 2.4.1.235 created 2004, deleted 2006)]

EC 2.4.1.236

Accepted name: flavanone 7-O-glucoside 2''-O-β-L-rhamnosyltransferase

Reaction: UDP-β-L-rhamnose + a flavanone 7-O-β-D-glucoside = UDP + a flavanone 7-O-[α-L-rhamnosyl-(1→2)-β-D-glucoside]

See diagram for reaction with 7-O--glucosides of naringenin or apigenin or luteolin.

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

Other name(s): UDP-rhamnose:flavanone-7-O-glucoside-2''-O-rhamnosyltransferase; 1→2 UDP-rhamnosyltransferase; UDP-L-rhamnose:flavanone-7-O-glucoside 2''-O-β-L-rhamnosyltransferase

Systematic name: UDP-β-L-rhamnose:flavanone-7-O-glucoside 2''-O-α-L-rhamnosyltransferase

Comments: Acts on the 7-O-glucoside of naringenin and hesperetin, also the flavone 7-O-glucosides of luteolin and apigenin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125752-89-8

References:

1. Bar-Peled, M., Lewinsohn, E., Fluhr, R. and Gressel, J. UDP-rhamnose:flavanone-7-O-glucoside-2"-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus. J. Biol. Chem. 266 (1991) 20953-20959. [PMID: 1939145]

[EC 2.4.1.236 created 2004]

EC 2.4.1.237

Accepted name: flavonol 7-O-β-glucosyltransferase

Reaction: UDP-glucose + a flavonol = UDP + a flavonol 7-O-β-D-glucoside

For diagram click here.

Other name(s): UDP-glucose:flavonol 7-O-glucosyltransferase

Systematic name: UDP-glucose:flavonol 7-O-β-D-glucosyltransferase

Comments: Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a lesser extent on quercetin, kaempferol and myricetin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83682-90-0

References:

1. Stich, K., Halbwirth, H., Wurst, F. and Forkmann, G. UDP-glucose:flavonol 7-O-glucosyltransferase activity in flower extracts of Chrysanthemum segetum. Z. Naturforsch. [C] 52 (1997) 153-158. [PMID: 9167271]

[EC 2.4.1.237 created 2004]

EC 2.4.1.238

Accepted name: delphinidin 3,5-di-O-glucoside 3'-O-glucosyltransferase

Reaction: UDP-α-D-glucose + delphinidin 3,5-di-O-β-D-glucoside = UDP + delphinidin 3,3',5-tri-O-β-D-glucoside

For diagram of reaction click here.

Glossary: delphinidin = 3,3',4',5,5',7-hexahydroxyflavylium

Other name(s): UDP-glucose:anthocyanin 3'-O-glucosyltransferase; 3’GT

Systematic name: UDP-α-D-glucose:delphinidin-3,5-di-O-β-D-glucoside 3'-O-glucosyltransferase

Comments: Isolated from the plant Gentiana triflora (clustered gentian).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 380231-41-4

References:

1. Fukuchi-Mizutani, M., Okuhara, H., Fukui, Y., Nakao, M., Katsumoto, Y., Yonekura-Sakakibara, K., Kusumi, T., Hase, T. and Tanaka, Y. Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3'-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian. Plant Physiol. 132 (2003) 1652-1663. [PMID: 12857844]

[EC 2.4.1.238 created 2004, modified 2013]

EC 2.4.1.239

Accepted name: flavonol-3-O-glucoside glucosyltransferase

Reaction: UDP-glucose + a flavonol 3-O-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside

See diagram for reaction with 3-O-β-D-glucosides of kaempferol or quercetin.

Other name(s): UDP-glucose:flavonol-3-O-glucoside 2"-O-β-D-glucosyltransferase

Systematic name: UDP-glucose:flavonol-3-O-β-D-glucoside 2"-O-β-D-glucosyltransferase

Comments: One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240, flavonol-3-O-glycoside glucosyltransferase). TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly.

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

References:

1. Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434-443. [PMID: 6462109]

[EC 2.4.1.239 created 2004]

EC 2.4.1.240

Accepted name: flavonol-3-O-glycoside glucosyltransferase

Reaction: UDP-glucose + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside

See diagram for reaction with 3-O-β-D-glucosyl-(1→2)-β-D-glucosides of kaempferol or quercetin.

Systematic name: UDP-glucose:flavonol-3-O-β-D-glucosyl-(1→2)-β-D-glucoside 2'''-O-β-D-glucosyltransferase

Comments: One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase).

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

References:

1. Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434-443. [PMID: 6462109]

[EC 2.4.1.240 created 2004]

EC 2.4.1.241

Accepted name: digalactosyldiacylglycerol synthase

Reaction: UDP-α-D-galactose + 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol

For diagram click here.

Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase; UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase

Systematic name: UDP-α-D-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase

Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC 2.4.1.46, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.

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

References:

1. Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166-1173. [PMID: 11696551]

2. Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649-10654. [PMID: 10973486]

3. Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694-2706. [PMID: 14600212]

4. Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397-2400. [PMID: 15590685]

[EC 2.4.1.241 created 2005]

EC 2.4.1.242

Accepted name: NDP-glucose—starch glucosyltransferase

Reaction: NDP-glucose + [(1→4)-α-D-glucosyl]n = NDP + [(1→4)-α-D-glucosyl]n+1

Other name(s): granule-bound starch synthase; starch synthase II (ambiguous); waxy protein; starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase; granule-bound starch synthase I; GBSSI; granule-bound starch synthase II; GBSSII; GBSS; NDPglucose-starch glucosyltransferase

Systematic name: NDP-glucose:1,4-α-D-glucan 4-α-D-glucosyltransferase

Comments: Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-53-2

References:

1. Tsai, C.-Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11 (1974) 83-96. [PMID: 4824506]

2. Nakamura, T., Vrinten, P., Hayakawa, K. and Ikeda, J. Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 118 (1998) 451-459. [PMID: 9765530]

3. Fujita, N. and Taira, T. A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 207 (1998) 125-132. [PMID: 9951718]

4. Murai, J., Taira, T. and Ohta, D. Isolation and characterization of the three Waxy genes encoding the granule-bound starch synthase in hexaploid wheat. Gene 234 (1999) 71-79. [PMID: 10393240]

5. Nelson, O.E. The waxy locus in maize. II The location of the controlling element alleles. Genetics 60 (1968) 507-524.

[EC 2.4.1.242 created 2005]

EC 2.4.1.243

Accepted name: 6G-fructosyltransferase

Reaction: [1-β-D-fructofuranosyl-(2→1)-]m+1 α-D-glucopyranoside + [1-β-D-fructofuranosyl-(2→1)-]n+1 α-D-glucopyranoside = [1-β-D-fructofuranosyl-(2→1)-]m α-D-glucopyranoside + [1-β-D-fructofuranosyl-(2→1)-]n+1 β-D-fructofuranosyl-(2→6)-α-D-glucopyranoside (m > 0; n ≥ 0)

Other name(s): fructan:fructan 6G-fructosyltransferase; 1F(1-β-D-fructofuranosyl)m sucrose:1F(1-β-D-fructofuranosyl)nsucrose 6G-fructosyltransferase; 6G-FFT; 6G-FT; 6G-fructotransferase

Systematic name: 1F-oligo[β-D-fructofuranosyl-(2→1)-]sucrose 6G-β-D-fructotransferase

Comments: Inulins are polysaccharides consisting of linear or branched D-fructofuranosyl chains attached to the fructosyl residue of sucrose by a β(2→1) linkage. This enzyme catalyses the transfer of the terminal (2→1)-linked -D-fructosyl group of an inulin chain onto O-6 position of the glucose residue of another inulin molecule [1]. For example, if 1-kestose [1F-(β-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-di-β-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see 2-Carb-36.2). Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. Side reactions catalysed are transfer of a β-D-fructosyl group between compounds of the structure 1F-(1-β-D-fructofuranosyl)m-6G-(1-β-D-fructofuranosyl)n sucrose, where m ≥ 0 and n = 1 for the donor, and m ≥ 0 and n ≥ 0 for the acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 79633-28-6

References:

1. Shiomi, N. Purification and characterisation of 6G-fructosyltransferase from the roots of asparagus (Asparagus officinalis L.). Carbohydr. Res. 96 (1981) 281-292.

2. Shiomi, N. Reverse reaction of fructosyl transfer catalysed by asparagus 6G-fructosyltransferase. Carbohydr. Res. 106 (1982) 166-169.

3. Shiomi, N. and Ueno, K. Cloning and expression of genes encoding fructosyltransferases from higher plants in food technology. J. Appl. Glycosci. 51 (2004) 177-183.

4. Ueno, K., Onodera, S., Kawakami, A., Yoshida, M. and Shiomi, N. Molecular characterization and expression of a cDNA encoding fructan:fructan 6G-fructosyltransferase from asparagus (Asparagus officinalis). New Phytol. 165 (2005) 813-824. [PMID: 15720693]

[EC 2.4.1.243 created 2006]

EC 2.4.1.244

Accepted name: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group

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

Other name(s): β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase

Comments: The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group.

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

References:

1. Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534-47544. [PMID: 12966086]

2. Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of β1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134-140. [PMID: 15044014]

[EC 2.4.1.244 created 2006]

EC 2.4.1.245

Accepted name: α,α-trehalose synthase

Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP

Glossary: NDP = a nucleoside diphosphate

Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase

Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase

Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].

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

References:

1. Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890-47897. [PMID: 15364950]

2. Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429-436. [PMID: 15737605]

3. Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939-7946. [PMID: 18835983]

4. Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355-369. [PMID: 18483808]

[EC 2.4.1.245 created 2008, modified 2013]

EC 2.4.1.246

Accepted name: mannosylfructose-phosphate synthase

Reaction: GDP-mannose + D-fructose 6-phosphate = GDP + β-D-fructofuranosyl-α-D-mannopyranoside 6F-phosphate

Glossary: mannosylfructose = β-D-fructofuranosyl-α-D-mannopyranoside

Other name(s): mannosylfructose-6-phosphate synthase; MFPS

Systematic name: GDP-mannose:D-fructose-6-phosphate 2-α-D-mannosyltransferase

Comments: This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg2+ or Mn2+ for activity. GDP-mannose can be replaced by ADP-mannose but with a concomitant decrease in activity. The product of this reaction is dephosphorylated by EC 3.1.3.79 (mannosylfructose-phosphate phosphatase) to form the non-reducing disaccharide mannosylfructose, which is the major endogenous osmolyte produced by several α-proteobacteria in response to osmotic stress. The F in the product name is used to indicate that the fructose residue of sucrose carries the substituent.

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

References:

1. Torres, L.L. and Salerno, G.L. A metabolic pathway leading to mannosylfructose biosynthesis in Agrobacterium tumefaciens uncovers a family of mannosyltransferases. Proc. Natl. Acad. Sci. USA 104 (2007) 14318–14323. [PMID: 17728402]

[EC 2.4.1.246 created 2009]

EC 2.4.1.247

Accepted name: β-D-galactosyl-(1→4)-L-rhamnose phosphorylase

Reaction: β-D-galactosyl-(1→4)-L-rhamnose + phosphate = L-rhamnose + α-D-galactose 1-phosphate

Other name(s): D-galactosyl-β1→4-L-rhamnose phosphorylase; GalRhaP

Systematic name: β-D-galactosyl-(1→4)-L-rhamnose:phosphate 1-α-D-galactosyltransferase

Comments: The enzyme from Clostridium phytofermentans is also active towards towards β-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order. Differs from 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active towards L-rhamnose and inactive towards N-acetyl hexosamine derivatives.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 1236189-79-9

References:

1. Nakajima, M., Nishimoto, M. and Kitaoka, M. Characterization of three β-galactoside phosphorylases from Clostridium phytofermentans: discovery of D-galactosyl-β1→4-L-rhamnose phosphorylase. J. Biol. Chem. 284 (2009) 19220-19227. [PMID: 19491100]

[EC 2.4.1.247 created 2009]

EC 2.4.1.248

Accepted name: cycloisomaltooligosaccharide glucanotransferase

Reaction: cyclizes part of a (1→6)-α-D-glucan chain by formation of a (1→6)-α-D-glucosidic bond

Systematic name: (1→6)-α-D-glucan:(1→6)-α-D-glucan 6-α-D-[1→6α-D-glucano]-transferase (cyclizing)

Comments: Specific for (1→6)-α-D-glucans (dextrans) and, unlike cyclomaltodextrin glucanotransferase (EC 2.4.1.19), without activity towards (1→4)-α-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1→6)-α-D-glucosidic linkages at branch points. The enzyme from Bacillus circulans T-3040 has been shown to form cycloisomalto-oligosaccharides of three sizes (7, 8 and 9 glucose units). It will also catalyse the disproportionation of two isomalto-oligosaccharides molecules to yield a series of isomalto-oligosachharides and the addition of D-glucose to cycloisomalto-oligosaccharides with ring opening to form isomalto-oligosaccharides.

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

References:

1. Oguma T, Horiuchi, T, and Kobayashi M. Novel Cyclic dextrins, Cycloisomaltooligosaccharides, from Bacillus sp. T-3040 culture. Biosci. Biotech. Biochem. 57 (1993) 1225-1227.

2. Oguma, T., Tobe, K. and Kobayashi, M. Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides. FEBS Lett. 345 (1994) 135-138. [PMID: 7515357]

3. Yamamoto, T., Terasawa, K., Kim, Y.M., Kimura, A., Kitamura, Y., Kobayashi, M. and Funane, K. Identification of catalytic amino acids of cyclodextran glucanotransferase from Bacillus circulans T-3040. Biosci. Biotechnol. Biochem. 70 (2006) 1947-1953. [PMID: 16926507]

[EC 2.4.1.248 created 2009]

EC 2.4.1.249

Accepted name: delphinidin 3',5'-O-glucosyltransferase

Reaction: 2 UDP-glucose + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside = 2 UDP + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3',5'-di-O-β-D-glucoside (overall reaction)
(1a) UDP-glucose + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside = UDP + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3'-O-β-D-glucoside
(1b) UDP-glucose + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3'-O-β-D-glucoside = UDP + delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3',5'-di-O-β-D-glucoside

For diagram of reaction click here.

Glossary: delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3',5'-di-O-β-D-glucoside = ternatin C5.

Other name(s): UDP-glucose:anthocyanin 3',5'-O-glucosyltransferase; UA3'5’GZ

Systematic name: UDP-glucose:delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside 3'-O-glucosyltransferase

Comments: Ternatins are a group of polyacetylated delphinidin glucosides that confer blue color to the petals of butterfly pea (Clitoria ternatea). This enzyme catalyses two reactions in the biosynthesis of ternatin C5: the conversion of delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside to delphinidin 3-O-(6"-O-malonyl)-β-D-glucoside-3'-O-β-D-glucoside, followed by the conversion of the later to ternatin C5, by transferring two glucosyl groups in a stepwise manner [1].

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

References:

1. Kogawa, K., Kato, N., Kazuma, K., Noda, N. and Suzuki, M. Purification and characterization of UDP-glucose: anthocyanin 3',5'-O-glucosyltransferase from Clitoria ternatea. Planta 226 (2007) 1501-1509. [PMID: 17668234]

[EC 2.4.1.249 created 2009]

EC 2.4.1.250

Accepted name: D-inositol-3-phosphate glycosyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP

For diagram of reaction click here

Other name(s): mycothiol glycosyltransferases; MshA

Systematic name: UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase

Comments: The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3]

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

References:

1. Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476-3479. [PMID: 12754249]

2. Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910-33920. [PMID: 16940050]

3. Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834-15844. [PMID: 18390549]

[EC 2.4.1.250 created 2010]


Continued with EC 2.4.1.251-EC 2.4.1.300
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