Enzyme Nomenclature

EC 2.4.1 (continued)

Hexosyltransferases

Continued from EC 2.4.1.1 to EC 2.4.1.50

See separate file for 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, EC 2.4.1.251 to EC 2.4.1.300 and EC 2.4.1.301 to EC 2.4.1.374.

Contents

EC 2.4.1.51 now covered by EC 2.4.1.101, EC 2.4.1.143, EC 2.4.1.144 and EC 2.4.1.145
EC 2.4.1.52 poly(glycerol-phosphate) α-glucosyltransferase
EC 2.4.1.53 poly(ribitol-phosphate) β-glucosyltransferase
EC 2.4.1.54 undecaprenyl-phosphate mannosyltransferase
EC 2.4.1.55 now EC 2.7.8.14
EC 2.4.1.56 lipopolysaccharide N-acetylglucosaminyltransferase
EC 2.4.1.57 deleted now covered by EC 2.4.1.345 and EC 2.4.1.346
EC 2.4.1.58 lipopolysaccharide glucosyltransferase I
EC 2.4.1.59 deleted, included in EC 2.4.1.17
EC 2.4.1.60 abequosyltransferase
EC 2.4.1.61 deleted, included in EC 2.4.1.17
EC 2.4.1.62 ganglioside galactosyltransferase
EC 2.4.1.63 linamarin synthase
EC 2.4.1.64 α,α-trehalose phosphorylase
EC 2.4.1.65 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase
EC 2.4.1.66 procollagen glucosyltransferase
EC 2.4.1.67 galactinol—raffinose galactosyltransferase
EC 2.4.1.68 glycoprotein 6-α-L-fucosyltransferase
EC 2.4.1.69 type 1 galactoside α-(1,2)-fucosyltransferase
EC 2.4.1.70 poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase
EC 2.4.1.71 arylamine glucosyltransferase
EC 2.4.1.72 now EC 2.4.2.24
EC 2.4.1.73 lipopolysaccharide glucosyltransferase II
EC 2.4.1.74 glycosaminoglycan galactosyltransferase
EC 2.4.1.75 deleted entry
EC 2.4.1.76 deleted, included in EC 2.4.1.17
EC 2.4.1.77 deleted, included in EC 2.4.1.17
EC 2.4.1.78 phosphopolyprenol glucosyltransferase
EC 2.4.1.79 globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase
EC 2.4.1.80 ceramide glucosyltransferase
EC 2.4.1.81 flavone 7-O-β-glucosyltransferase
EC 2.4.1.82 galactinol-sucrose galactosyltransferase
EC 2.4.1.83 dolichyl-phosphate β-D-mannosyltransferase
EC 2.4.1.84 deleted, included in EC 2.4.1.17
EC 2.4.1.85 cyanohydrin β-glucosyltransferase
EC 2.4.1.86 N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase
EC 2.4.1.87 N-acetyllactosaminide 3-α-galactosyltransferase
EC 2.4.1.88 globoside α-N-acetylgalactosaminyltransferase
EC 2.4.1.89 deleted, included in EC 2.4.1.69
EC 2.4.1.90 N-acetyllactosamine synthase
EC 2.4.1.91 flavonol 3-O-glucosyltransferase
EC 2.4.1.92 (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase
EC 2.4.1.93 now EC 4.2.2.18
EC 2.4.1.94 protein N-acetylglucosaminyltransferase
EC 2.4.1.95 deleted
EC 2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase
EC 2.4.1.97 1,3-β-D-glucan phosphorylase
EC 2.4.1.98 deleted, included in EC 2.4.1.90
EC 2.4.1.99 sucrose:sucrose fructosyltransferase
EC 2.4.1.100 2,1-fructan:2,1-fructan 1-fructosyltransferase

See the following files for:
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
EC 2.4.1.251 to EC 2.4.1.300
EC 2.4.1.301 to EC 2.4.1.374

Entries

[EC 2.4.1.51 Deleted entry: UDP-N-acetylglucosamine—glycoprotein N-acetylglucosaminyltransferase. Now listed as EC 2.4.1.101 (α-1,3-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase), EC 2.4.1.143 (α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase), EC 2.4.1.144 (β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase) and EC 2.4.1.145 (α-1,3-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase) (EC 2.4.1.51 created 1972, deleted 1984)]

EC 2.4.1.52

Accepted name: poly(glycerol-phosphate) α-glucosyltransferase

Reaction: n UDP-α-D-glucose + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-{poly[(2R)-2-α-D-glucosyl-1-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): UDP glucose-poly(glycerol-phosphate) α-glucosyltransferase; uridine diphosphoglucose-poly(glycerol-phosphate) α-glucosyltransferase; tagE (gene name); UDP-glucose:poly(glycerol-phosphate) α-D-glucosyltransferase

Systematic name: UDP-α-D-glucose:4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol α-D-glucosyltransferase (configuration-retaining)

Comments: Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme, isolated from Bacillus subtilis 168, adds an α-D-glucose to the free OH groups of the glycerol units. The enzyme has a strong preference for UDP-α-glucose as the sugar donor. It has no activity with poly(ribitol phosphate).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-60-4

References:

1. Glaser, L. and Burger, M.M. The synthesis of teichoic acids. 3. Glucosylation of polyglycerophosphate. J. Biol. Chem. 239 (1964) 3187-3191. [PMID: 14245359]

2. Allison, S.E., D'Elia, M.A., Arar, S., Monteiro, M.A. and Brown, E.D. Studies of the genetics, function, and kinetic mechanism of TagE, the wall teichoic acid glycosyltransferase in Bacillus subtilis 168. J. Biol. Chem. 286 (2011) 23708-23716. [PMID: 21558268]

[EC 2.4.1.52 created 1972, modified 2017]

EC 2.4.1.53

Accepted name: poly(ribitol-phosphate) β-glucosyltransferase

Reaction: n UDP-α-D-glucose + 4-O-[(1-D-ribitylphospho)n-(1-D-ribitylphospho)-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-[(2-β-D-glucosyl-1-D-ribitylphospho)n-(1-D-ribitylphospho)-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): TarQ; UDP glucose-poly(ribitol-phosphate) β-glucosyltransferase; uridine diphosphoglucose-poly(ribitol-phosphate) β-glucosyltransferase; UDP-D-glucose polyribitol phosphate glucosyl transferase; UDP-D-glucose:polyribitol phosphate glucosyl transferase; UDP-glucose:poly(ribitol-phosphate) β-D-glucosyltransferase

Systematic name: UDP-α-D-glucose:4-O-[(1-D-ribitylphospho)n-(1-D-ribitylphospho)-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-D-glucosyltransferase (cofiguration-inverting)

Comments: Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Bacillus subtilis W23. This enzyme adds a β-D-glucose to the hydroxyl group at the 2 position of the ribitol phosphate units.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-61-5

References:

1. Chin, T., Burger, M.M. and Glaser, L. Synthesis of teichoic acids. VI. The formation of multiple wall polymers in Bacillus subtilis W-23. Arch. Biochem. Biophys. 116 (1966) 358-367. [PMID: 4960203]

2. Brown, S., Xia, G., Luhachack, L.G., Campbell, J., Meredith, T.C., Chen, C., Winstel, V., Gekeler, C., Irazoqui, J.E., Peschel, A. and Walker, S. Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids. Proc. Natl Acad. Sci. USA 109 (2012) 18909-18914. [PMID: 23027967]

[EC 2.4.1.53 created 1972, modified 2018]

EC 2.4.1.54

Accepted name: undecaprenyl-phosphate mannosyltransferase

Reaction: GDP-mannose + undecaprenyl phosphate = GDP + D-mannosyl-1-phosphoundecaprenol

Other name(s): guanosine diphosphomannose-undecaprenyl phosphate mannosyltransferase; GDP mannose-undecaprenyl phosphate mannosyltransferase; GDP-D-mannose:lipid phosphate transmannosylase

Systematic name: GDP-mannose:undecaprenyl-phosphate D-mannosyltransferase

Comments: Requires phosphatidylglycerol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-62-6

References:

1. Lahav, M., Chiu, T.H. and Lennarz, W.J. Studies on the biosynthesis of mannan in Micrococcus lysodeikticus. II. The enzymatic synthesis of mannosyl-l-phosphoryl-undecaprenol. J. Biol. Chem. 244 (1969) 5890-5898. [PMID: 5350943]

[EC 2.4.1.54 created 1972]

[EC 2.4.1.55 Transferred entry: now EC 2.7.8.14 CDP-ribitol ribitolphosphotransferase (EC 2.4.1.55 created 1972, deleted 1982)]

EC 2.4.1.56

Accepted name: lipopolysaccharide N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-α-D-glucosamine + lipopolysaccharide = UDP + N-acetyl-D-glucosaminyllipopolysaccharide

Other name(s): UDP-N-acetylglucosamine-lipopolysaccharide N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lipopolysaccharide acetylglucosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-glucosamine:lipopolysaccharide N-acetyl-D-glucosaminyltransferase

Comments: Transfers N-acetylglucosaminyl residues to a D-galactose residue in the partially completed lipopolysaccharide core [cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase), EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-64-8

References:

1. Osborn, M.J. and D'Ari, L. Enzymatic incorporation of N-acetylglucosamine into cell wall lipopolysaccharide in a mutant strain of Salmonella typhimurium. Biochem. Biophys. Res. Commun. 16 (1964) 568-575.

[EC 2.4.1.56 created 1972]

[EC 2.4.1.57 Deleted entry: phosphatidylinositol α-mannosyltransferase. Newer studies have shown that this is catalysed by two independent activities now covered by EC 2.4.1.345, phosphatidyl-myo-inositol α-mannosyl transferase, and EC 2.4.1.346, phosphatidyl-myo-inositol dimannoside synthase (EC 2.4.1.57 created 1972, modified 2003, deleted 2017)]

EC 2.4.1.58

Accepted name: lipopolysaccharide glucosyltransferase I

Reaction: UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide

Other name(s): UDP-glucose:lipopolysaccharide glucosyltransferase I; lipopolysaccharide glucosyltransferase; uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I; uridine diphosphoglucose-lipopolysaccharide glucosyltransferase

Systematic name: UDP-glucose:lipopolysaccharide glucosyltransferase

Comments: Transfers glucosyl residues to the backbone portion of lipopolysaccharide [cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase, EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9074-00-4

References:

1. Müller, E., Hinckley, A. and Rothfield, L. Studies of phospholipid-requiring bacterial enzymes. 3. Purification and properties of uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I. J. Biol. Chem. 247 (1972) 2614-2622. [PMID: 4553445]

2. Rothfield, L., Osborn, M.J. and Horecker, B.L. Biosynthesis of bacterial lipopolysaccharide. II. Incorporation of glucose and galactose catalyzed by particulate and soluble enzymes in salmonella. J. Biol. Chem. 239 (1964) 2788-2795.

[EC 2.4.1.58 created 1972]

[EC 2.4.1.59 Deleted entry: UDP-glucuronate—estradiol glucuronosyltransferase. Now included with EC 2.4.1.17 UDP-glucuronosyltransferase (EC 2.4.1.59 created 1972, deleted 1984)]

EC 2.4.1.60

Accepted name: abequosyltransferase

Reaction: CDP-α-D-abequose + α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-β-D-galactopyranosyl-diphosphodecaprenol = CDP + α-D-abequopyranosyl-(1→3)-α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-β-D-galactopyranosyl-diphosphodecaprenol

Glossary: abequose = 3,6-deoxy-D-xylo-hexose = 3,6-deoxy-D-galactose = 3-deoxy-D-fucose

Other name(s): trihexose diphospholipid abequosyltransferase

Systematic name: CDP-α-D-abequose:Man(α1→4)Rha(α1→3)Gal(β-1)-diphospholipid D-abequosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-67-1

References:

1. Osborn, M.J. and Weiner, I.M. Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of incorporation of abequose into the O-antigen of Salmonella typhimurium. J. Biol. Chem. 243 (1968) 2631-2639. [PMID: 4297268]

2. Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084-4088. [PMID: 7541787]

[EC 2.4.1.60 created 1972, modified 2012]

[EC 2.4.1.61 Deleted entry: UDP-glucuronate—estriol 16α-glucuronosyltransferase. Now included with EC 2.4.1.17 UDP-glucuronosyltransferase (EC 2.4.1.61 created 1972, deleted 1984)]

EC 2.4.1.62

Accepted name: ganglioside galactosyltransferase

Reaction: UDP-α-D-galactose + an N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of reaction click here.

Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = ganglioside GM2
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a

Other name(s): UDP-galactose—ceramide galactosyltransferase; uridine diphosphogalactose-ceramide galactosyltransferase; UDP galactose-LAC Tet-ceramide α-galactosyltransferase; UDP-galactose-GM2 galactosyltransferase; uridine diphosphogalactose-GM2 galactosyltransferase; uridine diphosphate D-galactose:glycolipid galactosyltransferase; UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosyl-glucosyl-ceramide galactosyltransferase; UDP-galactose-GM2 ganglioside galactosyltransferase; GM1-synthase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine β-1,3-D-galactosyltransferase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine 3-β-D-galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase

Comments: The substrate is also known as gangloside GM2, the product as gangloside GM1a

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37217-28-0

References:

1. Basu, S., Kaufman, B. and Roseman, S. Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose: glycolipid galactosyltransferase. J. Biol. Chem. 240 (1965) 4115-4117. [PMID: 5842076]

2. Yip, G.B. and Dain, J.A. The enzymic synthesis of ganglioside. II. UDP-galactose: N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceramide galactosyltransferase in rat brain. Biochim. Biophys. Acta 206 (1970) 252-260. [PMID: 4987145]

3. Yip, M.C.M. and Dain, J.A. Frog brain uridine diphosphate galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosylceramide galactosyltransferase. Biochem. J. 118 (1970) 247-252. [PMID: 5484669]

[EC 2.4.1.62 created 1972, modified 2013]

EC 2.4.1.63

Accepted name: linamarin synthase

Reaction: UDP-glucose + 2-hydroxy-2-methylpropanenitrile = UDP + linamarin

Other name(s): uridine diphosphoglucose-ketone glucosyltransferase; uridine diphosphate-glucose-ketone cyanohydrin β-glucosyltransferase; UDP glucose ketone cyanohydrin glucosyltransferase; UDP-glucose:ketone cyanohydrin β-glucosyltransferase; uridine diphosphoglucose-ketone cyanohydrin glucosyltransferase

Systematic name: UDP-glucose:2-hydroxy-2-methylpropanenitrile β-D-glucosyltransferase

Comments: The enzyme glucosylates the cyanohydrins of butanone and pentan-3-one as well as that of acetone.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-68-2

References:

1. Hahlbrock, K. and Conn, E.E. The biosynthesis of cyanogenic glycosides in higher plants. I. Purification and properties of a uridine diphosphate-glucose-ketone cyanohydrin β-glucosyltransferase from Linum usitatissimum L. J. Biol. Chem. 245 (1970) 917-922. [PMID: 5417265]

[EC 2.4.1.63 created 1972]

EC 2.4.1.64

Accepted name: α,α-trehalose phosphorylase

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

For diagram of reaction click here

Other name(s): trehalose phosphorylase

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

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37205-59-7

References:

1. Belocopitow, E. and Maréchal, L.R. Trehalose phosphorylase from Euglena gracilis. Biochim. Biophys. Acta 198 (1970) 151-154. [PMID: 5413942]

[EC 2.4.1.64 created 1972]

EC 2.4.1.65

Accepted name: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(1→3)-[α-L-fucosyl-(1→4)]-N-acetyl-β-D-glucosaminyl-R

For diagram of reaction, click here

Other name(s): (Lea)-dependent (α-3/4)-fucosyltransferase; α(1,3/1,4) fucosyltransferase III; α-(1→4)-L-fucosyltransferase; α-4-L-fucosyltransferase; β-acetylglucosaminylsaccharide fucosyltransferase; FucT-II; Lewis α-(1→3/4)-fucosyltransferase; Lewis blood group α-(1→3/4)-fucosyltransferase; Lewis(Le) blood group gene-dependent α-(1→3/4)-L-fucosyltransferase; blood group Lewis α-4-fucosyltransferase; blood-group substance Lea-dependent fucosyltransferase; guanosine diphosphofucose-β-acetylglucosaminylsaccharide 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-fucosyltransferase; 3-α-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase; GDP-β-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase; GDP-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase

Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase

Comments: This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(1→3)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-69-3

References:

1. Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. Co-purification of the Lewis blood group N-acetylglucosaminide α1→4 fucosyltransferase and an N-acetylglucosaminide α1→3 fucosyltransferase from human milk. J. Biol. Chem. 256 (1981) 10456-10463. [PMID: 7287719]

2. Rasko, D.A., Wang, G., Palcic, M.M. and Taylor, D.E. Cloning and characterization of the α(1,3/4) fucosyltransferase of Helicobacter pylori. J. Biol. Chem. 275 (2000) 4988-4994. [PMID: 10671538]

3. Wilson, I.B.H. Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase. Glycoconj. J. 18 (2001) 439-447. [PMID: 12084979]

4. Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893-21900. [PMID: 12676935]

[EC 2.4.1.65 created 1972, modified 2001, modified twice 2002]

EC 2.4.1.66

Accepted name: procollagen glucosyltransferase

Reaction: UDP-α-D-glucose + [procollagen]-(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(2S,5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine

Other name(s): galactosylhydroxylysine glucosyltransferase; collagen glucosyltransferase; collagen hydroxylysyl glucosyltransferase; galactosylhydroxylysyl glucosyltransferase; UDP-glucose-collagenglucosyltransferase; uridine diphosphoglucose-collagen glucosyltransferase; UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase; UDP-glucose:(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] D-glucosyltransferase

Systematic name: UDP-α-D-glucose:[procollagen]-(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine 2-α-D-glucosyltransferase (configuration-retaining)

Comments: Probably involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.50 procollagen galactosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-08-4

References:

1. Bosmann, H.B. and Eylar, E.H. Attachment of carbohydrate to collagen. Isolation, purification and properties of the glucosyl transferase. Biochem. Biophys. Res. Commun. 30 (1968) 89-94. [PMID: 5637038]

2. Bosmann, H.B. and Eylar, E.H. Collagen-glucosyl transferase in fibriblasts transformed by oncogenic viruses. Nature 218 (1968) 582-583. [PMID: 4968368]

3. Butler, W.T. and Cunningham, L.W. Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen. J. Biol. Chem. 241 (1966) 3882-3888. [PMID: 4288358]

4. Kivirikko, K.I. and Myllyla, R. In: Hall, D.A. and Jackson, D.S. (Eds.), International Review of Connective Tissue Research, vol. 8, Academic Press, New York, 1979, p. 23.

5. Sricholpech, M., Perdivara, I., Nagaoka, H., Yokoyama, M., Tomer, K.B. and Yamauchi, M. Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J. Biol. Chem. 286 (2011) 8846-8856. [PMID: 21220425]

[EC 2.4.1.66 created 1972]

EC 2.4.1.67

Accepted name: galactinol—raffinose galactosyltransferase

Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + raffinose = myo-inositol + stachyose

For diagram of reaction click here.

Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside

Other name(s): galactinol-raffinose galactosyltransferase; stachyose synthetase; α-D-galactosyl-(1→3)-myo-inositol:raffinose galactosyltransferase

Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:raffinose galactosyltransferase

Comments: This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 3-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-70-6

References:

1. Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111 only.

2. Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233-239. [PMID: 5655499]

3. Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103-110. [PMID: 4774118]

4. Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant vol. 3, Academic Press, New York, 1980, pp. 221-270.

[EC 2.4.1.67 created 1972, modified 2003]

EC 2.4.1.68

Accepted name: glycoprotein 6-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→6)]-N-acetyl-β-D-glucosaminyl}asparagine

For diagram click here.

Other name(s): GDP-fucose—glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein 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) 6-α-L-fucosyltransferase; FucT; 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) 6-α-L-fucosyltransferase

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) 6-α-L-fucosyltransferase

Comments: This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-α-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-β-L-fucose to form an α1,6-linkage rather than an α1,3-linkage.

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

References:

1. Longmore, G.D. and Schachter, H. Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-β-D-glucoside (Fuc → Asn-linked GlcNAc) 6-α-L-fucosyltransferase in a Golgi-rich fraction from porcine liver. Carbohydr. Res. 100 (1982) 365-392. [PMID: 7083256]

2. Voynow, J.A., Scanlin, T.F. and Glick, M.C. A quantitative method for GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase activity with lectin affinity chromatography. Anal. Biochem. 168 (1988) 367-373. [PMID: 3364733]

3. Uozumi, N., Yanagidani, S., Miyoshi, E., Ihara, Y., Sakuma, T., Gao, C.-X., Teshima, T., Fujii, S., Shiba, T. and Taniguchi, N. Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1→6fucosyltransferase. J. Biol. Chem. 271 (1996) 27810-27817. [PMID: 8910378]

[EC 2.4.1.68 created 1972, modified 2002]

EC 2.4.1.69

Accepted name: type 1 galactoside α-(1,2)-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R

For diagram of reaction click here.

Other name(s): galactoside 2-α-L-fucosyltransferase (ambiguous); blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase; α-(1→2)-L-fucosyltransferase (ambiguous); α-2-fucosyltransferase (ambiguous); α-2-L-fucosyltransferase (ambiguous); blood-group substance H-dependent fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase (ambiguous); guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase (ambiguous); guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase (ambiguous); secretor-type β-galactoside α1→2fucosyltransferase; β-galactoside α1→2fucosyltransferase (ambiguous); GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT2 (gene name); GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 2-α-L-fucosyltransferase

Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R α-(1,2)-L-fucosyltransferase (configuration-inverting)

Comments: The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56093-23-3

References:

1. Beyer, T.A. and Hill, R.L. Enzymatic properties of the β-galactoside α1→2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5373-5379. [PMID: 7372640]

2. Beyer, T.A., Sadler, J.E. and Hill, R.L. Purification to homogeneity of H blood group β-galactoside α1→2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5364-5372. [PMID: 6246105]

3. Kumazaki, T. and Yoshida, A. Biochemical evidence that secretor gene, Se, is a structural gene encoding a specific fucosyltransferase. Proc. Natl. Acad. Sci. USA 81 (1984) 4193-4197. [PMID: 6588382]

4. Koda, Y., Soejima, M., Wang, B. and Kimura, H. Structure and expression of the gene encoding secretor-type galactoside 2-α-L-fucosyltransferase (FUT2). Eur. J. Biochem. 246 (1997) 750-755. [PMID: 9219535]

5. Wang, G., Boulton, P.G., Chan, N.W., Palcic, M.M. and Taylor, D.E. Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens. Microbiology 145 (1999) 3245-3253. [PMID: 10589734]

[EC 2.4.1.69 created 1972 (EC 2.4.1.89 created 1976, incorporated 1984), modified 2002, modified 2017]

EC 2.4.1.70

Accepted name: poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase

Reaction: n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-α-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s): TarM; UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); uridine diphosphoacetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase (ambiguous); UDP-N-acetyl-α-D-glucosamine:poly(ribitol-phosphate) N-acetyl-α-D-glucosaminyltransferase (ambiguous); poly(ribitol-phosphate) N-acetylglucosaminyltransferase (ambiguous)

Systematic name: UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)

Comments: Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-α-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.355 [poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-71-7

References:

1. Nathenson, S.G., Ishimoto, N. and Strominger, J.L. UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases from Staphylococcus aureus. Methods Enzymol. 8 (1966) 426-429.

2. Xia, G., Maier, L., Sanchez-Carballo, P., Li, M., Otto, M., Holst, O. and Peschel, A. Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM. J. Biol. Chem. 285 (2010) 13405-13415. [PMID: 20185825]

3. Sobhanifar, S., Worrall, L.J., Gruninger, R.J., Wasney, G.A., Blaukopf, M., Baumann, L., Lameignere, E., Solomonson, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase. Proc. Natl Acad. Sci. USA 112 (2015) E576-E585. [PMID: 25624472]

4. Koc, C., Gerlach, D., Beck, S., Peschel, A., Xia, G. and Stehle, T. Structural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid. J. Biol. Chem. 290 (2015) 9874-9885. [PMID: 25697358]

[EC 2.4.1.70 created 1972, modified 2018]

EC 2.4.1.71

Accepted name: arylamine glucosyltransferase

Reaction: UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine

Other name(s): UDP glucose-arylamine glucosyltransferase; uridine diphosphoglucose-arylamine glucosyltransferase

Systematic name: UDP-glucose:arylamine N-D-glucosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37277-72-8

References:

1. Frear, D.S. Herbicide metabolism in plants. I. Purification and properties of UDP-glucose:arylamine N-glucosyl-transferase from soybean. Phytochemistry 7 (1968) 381-390.

[EC 2.4.1.71 created 1972]

[EC 2.4.1.72 Transferred entry: now EC 2.4.2.24 1,4-β-D-xylan synthase (EC 2.4.1.72 created 1972, deleted 1976)]

EC 2.4.1.73

Accepted name: lipopolysaccharide glucosyltransferase II

Reaction: UDP-glucose + lipopolysaccharide = UDP + α-D-glucosyl-lipopolysaccharide

Other name(s): uridine diphosphoglucose-galactosylpolysaccharide glucosyltransferase

Systematic name: UDP-glucose:galactosyl-lipopolysaccharide α-D-glucosyltransferase

Comments: Transfers glucosyl residues to the D-galactosyl-D-glucosyl side-chains in the partially completed core of lipopolysaccharides. cf. EC 2.4.1.44 (lipopolysaccharide 3-α-galactosyltransferase), EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.58 (lipopolysaccharide glucosyltransferase I).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51004-27-4

References:

1. Edstrom, R.D. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. VI. Enzymatic transfer of galactose, glucose, N-acetylglucosamine, and colitose into the polymer. J. Biol. Chem. 242 (1967) 3581-3588. [PMID: 5341482]

[EC 2.4.1.73 created 1972]

EC 2.4.1.74

Accepted name: glycosaminoglycan galactosyltransferase

Reaction: UDP-α-D-galactose + glycosaminoglycan = UDP + D-galactosylglycosaminoglycan

Other name(s): uridine diphosphogalactose-mucopolysaccharide galactosyltransferase; UDP-galactose:glycosaminoglycan D-galactosyltransferase

Systematic name: UDP-α-D-galactose:glycosaminoglycan D-galactosyltransferase

Comments: Involved in the biosynthesis of galactose-containing glycosaminoglycan of Dictyostelium discoideum.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51004-28-5

References:

1. Sussman, M. and Osborn, M.J. UDP-glucose polysaccharide transferase in the cellular slime mold Dictyostelium discoideum: appearance and dissappearance of activity during cell differentiation. Proc. Natl. Acad. Sci. USA 52 (1964) 81-87.

[EC 2.4.1.74 created 1972, modified 1980]

[EC 2.4.1.75 Deleted entry: insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43, polygalacturonate 4-α-galacturonosyltransferase (EC 2.4.1.75 created 1976, deleted 2005)]

[EC 2.4.1.76 Deleted entry: UDP-glucuronate—bilirubin glucuronosyltransferase. Now included with EC 2.4.1.17, UDP-glucuronosyltransferase (EC 2.4.1.76 created 1976, deleted 1984)]

[EC 2.4.1.77 Deleted entry: UDP-glucuronate—bilirubin-glucuronoside glucuronosyltransferase. Now included with EC 2.4.1.17, UDP-glucuronosyltransferase (EC 2.4.1.77 created 1976, deleted 1984)]

EC 2.4.1.78

Accepted name: phosphopolyprenol glucosyltransferase

Reaction: UDP-glucose + undecaprenyl phosphate = UDP + β-D-glucosyl-1-phosphoundecaprenol

Other name(s): gtrB (gene name); bactoprenol glucosyl transferase; polyisoprenyl-phosphate glycosyltransferase; uridine diphosphoglucose-polyprenol monophosphate glucosyltransferase; UDP-glucose:polyprenol monophosphate glucosyltransferase

Systematic name: UDP-glucose:undecaprenyl-phosphate D-glucosyltransferase (configuration- inverting)

Comments: The enzyme, characterized from the bacterium Shigella flexneri and its bacteriophages, catalyses the transfer of the glucose residue from UDP-glucose to the lipid carrier undecaprenyl phosphate. Following the flipping of the lipid-bound glucose across the cytoplasmic membrane, the glucose is used in the synthesis of the organism’s O-glycan in the periplasm.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55576-46-0

References:

1. Jankowski, W., Mankowski, T. and Chojnacki, T. Formation of polyprenol monophosphate glucose in Shigella flexneri. Biochim. Biophys. Acta 337 (1974) 153-162. [PMID: 4373050]

2. Mavris, M., Manning, P.A. and Morona, R. Mechanism of bacteriophage SfII-mediated serotype conversion in Shigella flexneri. Mol. Microbiol. 26 (1997) 939-950. [PMID: 9426131]

3. Allison, G.E. and Verma, N.K. Serotype-converting bacteriophages and O-antigen modification in Shigella flexneri. Trends Microbiol 8 (2000) 17-23. [PMID: 10637639]

4. Ardiccioni, C., Clarke, O.B., Tomasek, D., Issa, H.A., von Alpen, D.C., Pond, H.L., Banerjee, S., Rajashankar, K.R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., Manzini, M.C., Shapiro, L. and Mancia, F. Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun 7 (2016) 10175. [PMID: 26729507]

[EC 2.4.1.78 created 1976]

EC 2.4.1.79

Accepted name: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase

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

For diagram of reaction click here.

Glossary: globotriaosylceramide = Pk antigen = α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide
globotetraosylceramide = globoside = P antigen = β-N-acetyl-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide

Other name(s): uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine:globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase; globoside synthase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide β-N-acetyl-D-galactosaminyltransferase; β3GalNAc-T1; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3III-β-N-acetyl-D-galactosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase

Comments: Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted '3' in the systematic name, see GL-5.3.4.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-46-1

References:

1. Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778-1785. [PMID: 4632917]

2. Ishibashi, T., Kijimoto, S. and Makita, A. Biosynthesis of globoside and Forssman hapten from trihexosylceramide and properties of β-N-acetyl-galactosaminyltransferase of guinea pig kidney. Biochim. Biophys. Acta 337 (1974) 92-106. [PMID: 4433547]

3. Taniguchi, N. and Makita, A. Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide β-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen. J. Biol. Chem. 259 (1984) 5637-5642. [PMID: 6425294]

4. Okajima, T., Nakamura, Y., Uchikawa, M., Haslam, D.B., Numata, S.I., Furukawa, K., Urano, T. and Furukawa, K. Expression cloning of human globoside synthase cDNAs. Identification of β3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase. J. Biol. Chem. 275 (2000) 40498-40503. [PMID: 10993897]

[EC 2.4.1.79 created 1976, (EC 2.4.1.154 incorporated 2006), modified 2006]

EC 2.4.1.80

Accepted name: ceramide glucosyltransferase

Reaction: UDP-α-D-glucose + an N-acylsphingosine = UDP + a D-glucosyl-N-acylsphingosine

For diagram of reaction click here.

Other name(s): UDP-glucose:ceramide glucosyltransferase; ceramide:UDP-Glc glucosyltransferase; uridine diphosphoglucose-ceramide glucosyltransferase; ceramide:UDP-glucose glucosyltransferase; glucosylceramide synthase; UDP-glucose:N-acylsphingosine D-glucosyltransferase

Systematic name: UDP-α-D-glucose:N-acylsphingosine D-glucosyltransferase

Comments: Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37237-44-8

References:

1. Basu, S., Kaufman, B. and Roseman, S. Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1388-1394. [PMID: 4631392]

[EC 2.4.1.80 created 1976]

EC 2.4.1.81

Accepted name: flavone 7-O-β-glucosyltransferase

Reaction: UDP-glucose + 5,7,3',4'-tetrahydroxyflavone = UDP + 7-O-β-D-glucosyl-5,7,3',4'-tetrahydroxyflavone

See diagram for reaction on apigenin or luteolin.

Other name(s): UDP-glucose—apigenin β-glucosyltransferase; UDP-glucose-luteolin β-D-glucosyltransferase; uridine diphosphoglucose-luteolin glucosyltransferase; uridine diphosphoglucose-apigenin 7-O-glucosyltransferase; UDP-glucosyltransferase (ambiguous)

Systematic name: UDP-glucose:5,7,3',4'-tetrahydroxyflavone 7-O-β-D-glucosyltransferase

Comments: A number of flavones, flavanones and flavonols can function as acceptors. Different from EC 2.4.1.91 (flavonol 3-O-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37332-50-6

References:

1. Sutter, A., Ortmann, R. and Grisebach, H. Purification and properties of an enzyme from cell suspension cultures of parsley catalyzing the transfer of D-glucose from UDP-D-glucose to flavonoids. Biochim. Biophys. Acta 258 (1972) 71-87. [PMID: 5058406]

[EC 2.4.1.81 created 1976]

EC 2.4.1.82

Accepted name: galactinol—sucrose galactosyltransferase

Reaction: α-D-galactosyl-(1→3)-1D-myo-inositol + sucrose = myo-inositol + raffinose

For diagram of reaction click here.

Glossary: raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside

Other name(s): 1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase; α-D-galactosyl-(1→3)-myo-inositol:sucrose 6-α-D-galactosyltransferase; raffinose synthase; RafS

Systematic name: α-D-galactosyl-(1→3)-1D-myo-inositol:sucrose 6-α-D-galactosyltransferase

Comments: 4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-45-0

References:

1. Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103-110. [PMID: 4774118]

2. Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494-1498. [PMID: 5491608]

[EC 2.4.1.82 created 1976, modified 2003]

EC 2.4.1.83

Accepted name: dolichyl-phosphate β-D-mannosyltransferase

Reaction: GDP-α-D-mannose + dolichyl phosphate = GDP + dolichyl β-D-mannosyl phosphate

For diagram of reaction click here.

Other name(s): GDP-Man:DolP mannosyltransferase; dolichyl mannosyl phosphate synthase; dolichyl-phospho-mannose synthase; GDP-mannose:dolichyl-phosphate mannosyltransferase; guanosine diphosphomannose-dolichol phosphate mannosyltransferase; dolichol phosphate mannose synthase; dolichyl phosphate mannosyltransferase; dolichyl-phosphate mannose synthase; GDP-mannose-dolichol phosphate mannosyltransferase; GDP-mannose-dolichylmonophosphate mannosyltransferase; mannosylphosphodolichol synthase; mannosylphosphoryldolichol synthase

Systematic name: GDP-mannose:dolichyl-phosphate β-D-mannosyltransferase

Comments: Acts only on long-chain polyprenyl phosphates and α-dihydropolyprenyl phosphates that are larger than C35.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-44-9

References:

1. Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509-515. [PMID: 6989607]

2. Bretthauer, R.K., Wu, S. and Irwin, W.E. Enzymatic transfer of mannose from guanosine diphosphate mannose to dolichol phosphate in yeast (Hansenula holstii). A possible step in mannan synthesis. Biochim. Biophys. Acta 304 (1973) 736-747. [PMID: 4726855]

3. Haselbeck, A. Purification of GDP mannose:dolichyl-phosphate O-β-D-mannosyltransferase from Saccharomyces cerevisiae. Eur. J. Biochem. 181 (1989) 663-668. [PMID: 2659345]

4. Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517-523. [PMID: 6445267]

5. Richards, J.B. and Hemming, F.W. The transfer of mannose from guanosine diphosphate mannose to dolichol phosphate and protein by pig liver endoplasmic reticulum. Biochem. J. 130 (1972) 77-93. [PMID: 4655455]

[EC 2.4.1.83 created 1976, modified 1983]

[EC 2.4.1.84 Deleted entry: UDP-glucuronate—1,2-diacylglycerol glucuronosyltransferase. Now included with EC 2.4.1.17, UDP-glucuronosyltransferase (EC 2.4.1.84 created 1976, deleted 1984)]

EC 2.4.1.85

Accepted name: cyanohydrin β-glucosyltransferase

Reaction: UDP-α-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile β-D-glucoside

For diagram click here.

Glossary: dhurrin = (S)-4-hydroxymandelonitrile β-D-glucoside

Other name(s): uridine diphosphoglucose-p-hydroxymandelonitrile glucosyltransferase; UDP-glucose-p-hydroxymandelonitrile glucosyltransferase; uridine diphosphoglucose-cyanohydrin glucosyltransferase; uridine diphosphoglucose:aldehyde cyanohydrin β-glucosyltransferase; UDP-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase; UGT85B1; UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase; UDP-D-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase

Systematic name: UDP-α-D-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase (configuration-inverting)

Comments: Acts on a wide range of substrates in vitro, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones, in a regiospecific manner [3]. This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.14.36, tyrosine N-monooxygenase and EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase. This reaction prevents the disocciation and release of toxic hydrogen cyanide [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55354-52-4

References:

1. Reay, P.F. and Conn, E.E. The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin β-glucosyltransferase from sorghum seedlings. J. Biol. Chem. 249 (1974) 5826-5830. [PMID: 4416442]

2. Jones, P.R., Møller, B.L. and Hoj, P.B. The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity. J. Biol. Chem. 274 (1999) 35483-35491. [PMID: 10585420]

3. Hansen, K.S., Kristensen, C., Tattersall, D.B., Jones, P.R., Olsen, C.E., Bak, S. and Møller, B.L. The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor. Phytochemistry 64 (2003) 143-151. [PMID: 12946413]

4. Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222-1231. [PMID: 12114576]

5. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784. [PMID: 15665094]

[EC 2.4.1.85 created 1976, modified 2005]

EC 2.4.1.86

Accepted name: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase

Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R

For diagram of reaction click here.

Other name(s): B3GALT1 (gene name); uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase; glucosaminylgalactosylglucosylceramide β-galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase

Comments: The enzyme transfers galactose from UDP-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-β-D-glucosamine (β-GlcNAc) residue. It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-46-5

References:

1. Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489-1495. [PMID: 4335001]

2. Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270-4274. [PMID: 291963]

3. Amado, M., Almeida, R., Carneiro, F., Levery, S.B., Holmes, E.H., Nomoto, M., Hollingsworth, M.A., Hassan, H., Schwientek, T., Nielsen, P.A., Bennett, E.P. and Clausen, H. A family of human β3-galactosyltransferases. Characterization of four members of a UDP-galactose:β-N-acetyl-glucosamine/β-nacetyl-galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 273 (1998) 12770-12778. [PMID: 9582303]

4. Amado, M., Almeida, R., Schwientek, T. and Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1473 (1999) 35-53. [PMID: 10580128]

5. Bardoni, A., Valli, M. and Trinchera, M. Differential expression of β1,3galactosyltransferases in human colon cells derived from adenocarcinomas or normal mucosa. FEBS Lett. 451 (1999) 75-80. [PMID: 10356986]

[EC 2.4.1.86 created 1976, modified 2017]

EC 2.4.1.87

Accepted name: N-acetyllactosaminide 3-α-galactosyltransferase

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

(where R can be OH, an oligosaccharide or a glycoconjugate)

Other name(s): α-galactosyltransferase; UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α-1,3-D-galactosyltransferase; UDP-Gal:Galβ1→4GlcNAc-R α1→3-galactosyltransferase; UDP-galactose-acetyllactosamine α-D-galactosyltransferase; UDPgalactose:β-D-galactosyl-β-1,4-N-acetyl-D-glucosaminyl-glycopeptide α-1,3-D-galactosyltransferase; glucosaminylglycopeptide α-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine α1→3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase; β-D-galactosyl-N-acetylglucosaminylglycopeptide α-1,3-galactosyltransferase; UDP-galactose:N-acetyllactosaminide 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-1,4-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase

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

Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 128449-51-4

References:

1. Basu, M. and Basu, S. Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an α-galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 248 (1973) 1700-1706. [PMID: 4632915]

2. Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α1→3Gal β1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927-12934. [PMID: 3932335]

3. Blake, D.A. and Goldstein, I.J. An α-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (α-D-galactose-(1→3)-N-acetyllactosamine). J. Biol. Chem. 256 (1981) 5387-5393. [PMID: 6787040]

[EC 2.4.1.87 created 1976, modified 1989, modified 2002 (EC 2.4.1.124 created 1984, incorporated 2002; EC 2.4.1.151 created 1984, incorporated 2002)

EC 2.4.1.88

Accepted name: globoside α-N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosylceramide = UDP + N-acetyl-D-galactosaminyl-(1→3)-N-acetyl-D-galactosaminyl-(1→3)-D-galactosyl-(1→4)-D-galactosyl-(1→4)-D-glucosylceramide

For diagram of reaction click here.

Other name(s): uridine diphosphoacetylgalactosamine-globoside α-acetylgalactosaminyltransferase; Forssman synthase; globoside acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide α-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide α-N-acetyl-D-galactosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide α-N-acetyl-D-galactosaminyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52037-97-5

References:

1. Kijimoto, S., Ishibashi, T. and Makita, A. Biosynthesis of Forssman hapten from globoside by α-N-acetylgalactosaminyltransferase of guinea pig tissues. Biochem. Biophys. Res. Commun. 56 (1974) 177-184. [PMID: 4823436]

[EC 2.4.1.88 created 1976]

[EC 2.4.1.89 Deleted entry: Galactosylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase - now included with EC 2.4.1.69 galactoside 2-L-fucosyltransferase (EC 2.4.1.89 created 1976, deleted 1984)]

EC 2.4.1.90

Accepted name: N-acetyllactosamine synthase

Reaction: UDP-α-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine

Other name(s): UDP-galactose—N-acetylglucosamine β-D-galactosyltransferase; uridine diphosphogalactose-acetylglucosamine galactosyltransferase; β-1,4-galactosyltransferase; acetyllactosamine synthetase; lactosamine synthase; lactosamine synthetase; lactose synthetase A protein; N-acetyllactosamine synthetase; UDP-galactose N-acetylglucosamine β-4-galactosyltransferase; UDP-galactose-acetylglucosamine galactosyltransferase; UDP-galactose-N-acetylglucosamine β-1,4-galactosyltransferase; UDP-galactose-N-acetylglucosamine galactosyltransferase; β1-4-galactosyltransferase; UDP-Gal:N-acetylglucosamine β1-4-galactosyltransferase; β1-4GalT; NAL synthetase; UDP-β-1,4-galactosyltransferase; Gal-T; UDP-galactose:N-acetylglucosaminide β1-4-galactosyltransferase; UDPgalactose:N-acetylglucosaminyl(β1-4)galactosyltransferase; β-N-acetylglucosaminide β1-4-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosamine 4-β-D-galactosyltransferase

Systematic name: UDP-α-D-galactose:N-acetyl-D-glucosamine 4-β-D-galactosyltransferase

Comments: The reaction is catalysed by a component of EC 2.4.1.22 (lactose synthase), which is identical with EC 2.4.1.38 (β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase), and by an enzyme from the Golgi apparatus of animal tissues. Formerly listed also as EC 2.4.1.98.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-94-8

References:

1. Deshmukh, D.S., Bear, W.D. and Soifer, D. Isolation and characterization of an enriched Golgi fraction from rat brain. Biochim. Biophys. Acta 542 (1978) 284-295. [PMID: 99178]

2. Helting, T. and Erbing, B. Galactosyl transfer in mouse mastocytoma: purification and properties of N-acetyllactosamine synthetase. Biochim. Biophys. Acta 293 (1973) 94-104. [PMID: 4631039]

3. Hill, R.L. and Brew, K. Lactose synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975) 411-490. [PMID: 812340]

4. Humphreys-Beher, M.G. Isolation and characterization of UDP-galactose:N-acetylglucosamine 4 β-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol. J. Biol. Chem. 259 (1984) 5797-5802. [PMID: 6201486]

5. Schachter, H., Jabbal, I., Hudgin, R.L., Pinteric, L., McGuire, E.J. and Roseman, S. Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction. J. Biol. Chem. 245 (1970) 1090-1100. [PMID: 4392041]

[EC 2.4.1.90 created 1976 (EC 2.4.1.98 created 1980, incorporated 1984)]

EC 2.4.1.91

Accepted name: flavonol 3-O-glucosyltransferase

Reaction: UDP-glucose + a flavonol = UDP + a flavonol 3-O-β-D-glucoside

See diagram for reaction on kaempferol or quercetin.

Other name(s): GTI; uridine diphosphoglucose-flavonol 3-O-glucosyltransferase; UDP-glucose:flavonol 3-O-glucosyltransferase; UDPG:flavonoid-3-O-glucosyltransferase

Systematic name: UDP-glucose:flavonol 3-O-D-glucosyltransferase

Comments: Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-β-glucosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50812-18-5

References:

1. Kleinehollenhorst, G., Behrens, H., Pegels, G., Srunk, N. and Wiermann, R. Formation of flavonol 3-O-diglycosides and flavonol 3-O-triglycosides by enzyme extracts from anthers of Tulipa cv apeldoorn - characterization and activity of 3 different O-glycosyltransferases during anther development. Z. Natursforsch. C: Biosci. 37 (1982) 587-599.

2. Sutter, A. and Grisebach, H. UDP-glucose: flavonol 3-O-glucosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 309 (1973) 289-295. [PMID: 4731963]

[EC 2.4.1.91 created 1976]

EC 2.4.1.92

Accepted name: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase

Reaction: UDP-N-acetyl-α-D-galactosamine + O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide = UDP + O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide

For diagram of reaction click here.

Glossary: ganglioside GM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminosyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide

ganglioside GM3 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide

ganglioside GD3 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→8)-O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide

ganglioside GD2 = 1-O-[O-(N-acetyl-α-neuraminosyl)-(2→8)-O-(N-acetyl-α-neuraminosyl)-(2→3)-O-[2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide

ganglioside SM3 = 1-O-[4-O-(3-O-sulfo-β-D-galactopyranosyl)-β-D-glucopyranosyl]-ceramide

ganglioside SM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-3-O-sulfo-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide

Other name(s): uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase; ganglioside GM2 synthase; ganglioside GM3 acetylgalactosaminyltransferase; GM2 synthase; UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase; GM2/GD2-synthase; β-1,4N-aetylgalactosaminyltransferase; asialo-GM2 synthase; GalNAc-T; UDP-N-acetyl-D-galactosamine:(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminosyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide (1→4)-β-N-acetyl-D-galactosaminyltransferase

Systematic name: UDP-N-acetyl-α-D-galactosamine:O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide 4-β-N-acetyl-D-galactosaminyltransferase

Comments: This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide [2] are also substrates, but glycoproteins and oligosaccharides are not substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 67338-98-1

References:

1. Dicesare, J.L. and Dain, J.A. The enzymic synthesis of ganglioside. IV. UDP-N-acetylgalactosamine: (N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyltransferase in rat brain. Biochim. Biophys. Acta 231 (1971) 385-393. [PMID: 5554906]

2. Pohlentz, G., Klein, D., Schwarzmann, G., Schmitz, D. and Sandhoff, K. Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proc. Natl. Acad. Sci. USA 85 (1988) 7044-7048. [PMID: 3140234]

3. Kazuya, I.-P., Hidari, J.K., Ichikawa, S., Furukawa, K., Yamasaki, M. and Hirabayashi, Y. β1-4N-Acetylgalactosaminyltransferase can synthesize both asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo: isolation and characterization of a β1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell line AH7974F. Biochem. J. 303 (1994) 957-965. [PMID: 7980468]

4. Hashimoto, Y., Sekine, M., Iwasaki, K. and Suzuki, A. Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver. J. Biol. Chem. 268 (1993) 25857-25864. [PMID: 8245020]

5. Nagai, K. and Ishizuka, I. Biosynthesis of monosulfogangliotriaosylceramide and GM2 by N-acetylgalactosaminyltransferase from rat brain. J. Biochem. (Tokyo) 101 (1987) 1115-1127. [PMID: 3115968]

6. Furukawa, K., Takamiya, K. and Furukawa, K. β1,4-N-Acetylgalactosaminyltransferase—GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides. Biochim. Biophys. Acta 1573 (2002) 356-362. [PMID: 12417418]

7. Yamashita, T., Wu, Y.P., Sandhoff, R., Werth, N., Mizukami, H., Ellis, J.M., Dupree, J.L., Geyer, R., Sandhoff, K. and Proia, R.L. Interruption of ganglioside synthesis produces central nervous system degeneration and altered axon-glial interactions. Proc. Natl. Acad. Sci. USA 102 (2005) 2725-2730. [PMID: 15710896]

[EC 2.4.1.92 created 1976, modified 2006]

[EC 2.4.1.93 Transferred entry: now EC 4.2.2.18, inulin fructotransferase (DFA-III-forming). The enzyme was wrongly classified as a transferase rather than a lyase. (EC 2.4.1.93 created 1976, deleted 2004)].

EC 2.4.1.94

Accepted name: protein N-acetylglucosaminyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + [protein]-L-asparagine = UDP + [protein]-N4-(N-acetyl-D-glucosaminyl)-L-asparagine

Other name(s): uridine diphosphoacetylglucosamine-protein acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase I

Systematic name: UDP-N-acetyl-D-glucosamine:[protein]-L-asparagine β-N-acetyl-D-glucosaminyl-transferase

Comments: The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-Thr or Asn-Xaa-Ser.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72319-34-7

References:

1. Khalkhali, Z. and Marshall, R.D. Glycosylation of ribonuclease A catalysed by rabbit liver extracts. Biochem. J. 146 (1975) 299-307. [PMID: 1156375]

2. Khalkhali, Z. and Marshall, R.D. UDP-N-acetyl-D-glucosamine-asparagine sequon N-acetyl-β-D-glucosaminyl-transferase-activity in human serum. Carbohydr. Res. 49 (1976) 455-473. [PMID: 986874]

3. Khalkhali, Z., Marshall, R.D., Reuvers, F., Habets-Willems, C. and Boer, P. Glycosylation in vitro of an asparagine sequon catalysed by preparations of yeast cell membranes. Biochem. J. 160 (1976) 37-41. [PMID: 795426]

[EC 2.4.1.94 created 1978, modified 2010]

[EC 2.4.1.95 Deleted entry: bilirubin-glucuronoside glucuronosyltransferase (EC 2.4.1.95 created 1978, deleted 2018)]

EC 2.4.1.96

Accepted name: sn-glycerol-3-phosphate 1-galactosyltransferase

Reaction: UDP-α-D-galactose + sn-glycerol 3-phosphate = UDP + 1-O-α-D-galactosyl-sn-glycerol 3-phosphate

Other name(s): isofloridoside-phosphate synthase; UDP-Gal:sn-glycero-3-phosphoric acid 1-α-galactosyl-transferase; UDPgalactose:sn-glycerol-3-phosphate α-D-galactosyltransferase; uridine diphosphogalactose-glycerol phosphate galactosyltransferase; glycerol 3-phosphate 1α-galactosyltransferase; UDP-galactose:sn-glycerol-3-phosphate 1-α-D-galactosyltransferase

Systematic name: UDP-α-D-galactose:sn-glycerol-3-phosphate 1-α-D-galactosyltransferase

Comments: The product is hydrolysed by a phosphatase to isofloridoside, which is involved in osmoregulation (cf. EC 2.4.1.137 sn-glycerol-3-phosphate 2-α-galactosyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-70-4

References:

1. Kauss, H. and Quader, H. In vitro activation of a galactosyl transferase involved in the osmotic regulation of Ochromonas. Plant Physiol. 58 (1976) 295-298. [PMID: 16659666]

2. Kauss, H. and Schubert, B. First demonstration of UDP-gal:sn-glycero-3-phosphoric acid 1α-galactosyl-transferase and its possible role in osmoregulation. FEBS Lett. 19 (1971) 131-135. [PMID: 11946194]

[EC 2.4.1.96 created 1978]

EC 2.4.1.97

Accepted name: 1,3-β-D-glucan phosphorylase

Reaction: [(1→3)-β-D-glucosyl]n + phosphate = [(1→3)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate

Other name(s): laminarin phosphoryltransferase; 1,3-β-D-glucan:orthophosphate glucosyltransferase

Systematic name: (1→3)-β-D-glucan:phosphate α-D-glucosyltransferase

Comments: Acts on a range of β-1,3-oligoglucans, and on glucans of laminarin type. Different from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.31 (laminaribiose phosphorylase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37340-31-1

References:

1. Albrecht, G.J. and Kauss, H. Purification, crystallization and properties of a β-(1→3)-glucan phosphorylase from Ochromonas malhamensis. Phytochemistry 10 (1971) 1293-1298.

[EC 2.4.1.97 created 1978]

[EC 2.4.1.98 Deleted entry: UDP-galactose—N-acetylglucosamine β-D-galactosyl-transferase. Now included with EC 2.4.1.90, N-acetyllactosamine synthase (EC 2.4.1.98 created 1980, deleted 1984)]

EC 2.4.1.99

Accepted name: sucrose:sucrose fructosyltransferase

Reaction: 2 sucrose = D-glucose + β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside

Other name(s): SST; sucrose:sucrose 1-fructosyltransferase; sucrose-sucrose 1-fructosyltransferase; sucrose 1F-fructosyltransferase; sucrose:sucrose 1F-β-D-fructosyltransferase

Systematic name: sucrose:sucrose 1'-β-D-fructosyltransferase

Comments: For definition of the prime in the systematic name, see 2-Carb-36.2

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73379-56-3

References:

1. Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017-1020.

2. Lüscher, M., Hochstrasser, U., Vogel, G., Aeschbacher, R., Galati, V., Nelson, C.J., Boller, T. and Wiemken, A. Cloning and functional analysis of sucrose:sucrose 1-fructosyltransferase from tall fescue. Plant Physiol 124 (2000) 1217-1228. [PMID: 11080298]

[EC 2.4.1.99 created 1981, modified 2004]

EC 2.4.1.100

Accepted name: 2,1-fructan:2,1-fructan 1-fructosyltransferase

Reaction: [β-D-fructosyl-(2→1)-]m + [β-D-fructosyl-(2→1)-]n = [β-D-fructosyl-(2→1)-]m-1 + [β-D-fructosyl-(2→1)-]n+1

Other name(s): 1,2-β-D-fructan 1F-fructosyltransferase; fructan:fructan fructosyl transferase; FFT; 1,2-β-fructan 1F-fructosyltransferase; 1,2-β-D-fructan:1,2-β-D-fructan 1F-β-D-fructosyltransferase; fructan:fructan 1-fructosyl transferase; 2,1-β-D-fructan:2,1-β-D-fructan 1-β-D-fructosyltransferase

Systematic name: (2→1)-β-D-fructan:(2→1)-β-D-fructan 1-β-D-fructosyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73379-55-2

References:

1. Henry, R.J. and Darbyshire, B. Sucrose:sucrose fructosyltransferase and fructan:fructan fructosyltransferase from Allium cepa. Phytochemistry 19 (1980) 1017-1020.

2. Vergauwen, R., Van Laere, A. and Van den Ende, W. Properties of fructan:fructan 1-fructosyltransferases from chicory and globe thistle, two asteracean plants storing greatly different types of inulin.Plant Physiol. 133 (2003) 391-401. [PMID: 12970504]

[EC 2.4.1.100 created 1981, modified 2004]


Continued with EC 2.4.1.101 to EC 2.4.1.150
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page