The Enzyme Database

Displaying entries 51-100 of 392.

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EC 2.4.1.45      
Deleted entry: 2-hydroxyacylsphingosine 1-β-galactosyltransferase, now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase
[EC 2.4.1.45 created 1972, deleted 2016]
 
 
EC 2.4.1.46     
Accepted name: monogalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose:diacylglycerol galactosyltransferase; MGDG synthase; UDP galactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose-diacylglyceride galactosyltransferase; UDP-galactose:1,2-diacylglycerol 3-β-D-galactosyltransferase; 1β-MGDG; 1,2-diacylglycerol 3-β-galactosyltransferase; UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Comments: This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241, digalactosyldiacylglycerol synthase, adds a galactosyl group to the product of the above reaction. There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-55-7
References:
1.  Veerkamp, J.H. Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides. Biochim. Biophys. Acta 348 (1974) 23–34. [DOI] [PMID: 4838219]
2.  Wenger, D.A., Petipas, J.W. and Pieringer, R.A. The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain. Biochemistry 7 (1968) 3700–3707. [PMID: 5681471]
3.  Miège, C., Maréchal, E., Shimojima, M., Awai, K., Block, M.A., Ohta, H., Takamiya, K., Douce, R. and Joyard, J. Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG. Eur. J. Biochem. 265 (1999) 990–1001. [DOI] [PMID: 10518794]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC 2.4.1.46 created 1972, modified 2003, modified 2005]
 
 
EC 2.4.1.47     
Accepted name: N-acylsphingosine galactosyltransferase
Reaction: UDP-α-D-galactose + a ceramide = UDP + a β-D-galactosylceramide
Glossary: a ceramide = an N-acylsphingosine
Other name(s): UGT8 (gene name); CGT (gene name); UDP galactose-N-acylsphingosine galactosyltransferase; uridine diphosphogalactose-acylsphingosine galactosyltransferase; UDP-galactose:N-acylsphingosine D-galactosyltransferase; UDP-α-D-galactose:N-acylsphingosine D-galactosyltransferase; 2-hydroxyacylsphingosine 1-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acylsphingosine β-D-galactosyltransferase (configuration-inverting)
Comments: This membrane-bound, endoplasmic reticulum-located enzyme catalyses the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. It has a strong preference for ceramides that contain hydroxylated fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-56-8
References:
1.  Fujino, Y. and Nakano, M. Enzymic synthesis of cerebroside from ceramide and uridine diphosphate galactose. Biochem. J. 113 (1969) 573–575. [PMID: 5807218]
2.  Morell, P. and Radin, N.S. Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid. Biochemistry 8 (1969) 506–512. [PMID: 5793706]
3.  Morell, P., Costantino-Ceccarini, E. and Radin, N.S. The biosynthesis by brain microsomes of cerebrosides containing nonhydroxy fatty acids. Arch. Biochem. Biophys. 141 (1970) 738–748. [DOI] [PMID: 5497154]
4.  Basu, S., Schultz, A., Basu, M. and Roseman, S. Enzymatic synthesis of galactocerebroside by a galactosyltransferase from embryonic chicken brain. J. Biol. Chem. 243 (1971) 4272–4279. [PMID: 5090043]
5.  Akanuma, H. and Kishimoto, Y. Synthesis of ceramides and cerebrosides containing both α-hydroxy and nonhydroxy fatty acids from lignoceroyl-CoA by rat brain microsomes. J. Biol. Chem. 254 (1979) 1050–1060. [PMID: 762114]
6.  Koul, O. and Jungalwala, F.B. UDP-galactose:ceramide galactosyltransferase of rat central-nervous-system myelin. Biochem. J. 194 (1981) 633–637. [PMID: 7306007]
7.  Schulte, S. and Stoffel, W. Ceramide UDP-galactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. USA 90 (1993) 10265–10269. [DOI] [PMID: 7694285]
8.  Sprong, H., Kruithof, B., Leijendekker, R., Slot, J.W., van Meer, G. and van der Sluijs, P. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. J. Biol. Chem. 273 (1998) 25880–25888. [DOI] [PMID: 9748263]
9.  Fewou, S.N., Bussow, H., Schaeren-Wiemers, N., Vanier, M.T., Macklin, W.B., Gieselmann, V. and Eckhardt, M. Reversal of non-hydroxy:α-hydroxy galactosylceramide ratio and unstable myelin in transgenic mice overexpressing UDP-galactose:ceramide galactosyltransferase. J. Neurochem. 94 (2005) 469–481. [DOI] [PMID: 15998297]
[EC 2.4.1.47 created 1972]
 
 
EC 2.4.1.50     
Accepted name: procollagen galactosyltransferase
Reaction: UDP-α-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine
Other name(s): hydroxylysine galactosyltransferase; collagen galactosyltransferase; collagen hydroxylysyl galactosyltransferase; UDP galactose-collagen galactosyltransferase; uridine diphosphogalactose-collagen galactosyltransferase; UDPgalactose:5-hydroxylysine-collagen galactosyltransferase; UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase; UDP-α-D-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase
Systematic name: UDP-α-D-galactose:[procollagen]-(5R)-5-hydroxy-L-lysine 5-β-D-galactosyltransferase (configuration-inverting)
Comments: Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.66 procollagen glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-07-3
References:
1.  Bosmann, H.B. and Eylar, E.H. Glycoprotein biosynthesis: the biosynthesis of the hydroxylysine-galactose linkage in collagen. Biochem. Biophys. Res. Commun. 33 (1968) 340–346. [DOI] [PMID: 5722225]
2.  Kivirikko, K.I. and Myllyla, R. In: Hall, D.A. and Jackson, D.S. (Ed.), International Review of Connective Tissue Research, vol. 8, Academic Press, New York, 1979, p. 23.
3.  Schegg, B., Hulsmeier, A.J., Rutschmann, C., Maag, C. and Hennet, T. Core glycosylation of collagen is initiated by two β(1-O)galactosyltransferases. Mol. Cell Biol. 29 (2009) 943–952. [DOI] [PMID: 19075007]
[EC 2.4.1.50 created 1972, modified 1983]
 
 
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 2-β-N-acetylglucosaminyltransferase), EC 2.4.1.143 (α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase), EC 2.4.1.144 (β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase) and EC 2.4.1.145 (α-1,3-mannosyl-glycoprotein 4-β-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. [DOI] [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 (configuration-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. [DOI] [PMID: 23027967]
[EC 2.4.1.53 created 1972, modified 2018]
 
 
EC 2.4.1.56     
Accepted name: lipopolysaccharide N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + lipopolysaccharide = UDP + N-acetyl-α-D-glucosaminyllipopolysaccharide
Other name(s): UDP-N-acetylglucosamine-lipopolysaccharide N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lipopolysaccharide acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:lipopolysaccharide N-acetyl-D-glucosaminyltransferase
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. [DOI] [PMID: 5332855]
[EC 2.4.1.56 created 1972]
 
 
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. [PMID: 14217875]
[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, glucuronosyltransferase
[EC 2.4.1.59 created 1972, deleted 1984]
 
 
EC 2.4.1.61      
Deleted entry:  UDP-glucuronate—estriol 16α-glucuronosyltransferase. Now included with EC 2.4.1.17, 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 ganglioside biosynthesis, 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. [DOI] [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 2.4.1.66     
Accepted name: procollagen glucosyltransferase
Reaction: UDP-α-D-glucose + [procollagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(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]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine 2-α-D-glucosyltransferase (configuration-retaining)
Comments: Involved in the synthesis of carbohydrate units in the complement system (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. [DOI] [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. (Ed.), 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. [DOI] [PMID: 21220425]
[EC 2.4.1.66 created 1972]
 
 
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. [DOI] [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. [DOI] [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. [DOI] [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 2.4.1.73     
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 the ameboid protozoan 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. [PMID: 14192661]
[EC 2.4.1.74 created 1972, modified 1980]
 
 
EC 2.4.1.75      
Deleted entry: UDP-galacturonosyltransferase. 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, 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, glucuronosyltransferase
[EC 2.4.1.77 created 1976, deleted 1984]
 
 
EC 2.4.1.78     
Accepted name: phosphopolyprenol glucosyltransferase
Reaction: UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose
Other name(s): uridine diphosphoglucose-polyprenol monophosphate glucosyltransferase; UDP-glucose:polyprenol monophosphate glucosyltransferase
Systematic name: UDP-glucose:phosphopolyprenol D-glucosyltransferase
Comments: Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, but more slowly.
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. [DOI] [PMID: 4373050]
[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 globotetraosylceramide biosynthesis, click here. For diagram of reaction, click here
Glossary: α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotriaosylceramide = Pk antigen
N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotetraosylceramide = globoside = P antigen
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; gUDP-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; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-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. [DOI] [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. [DOI] [PMID: 10993897]
[EC 2.4.1.79 created 1976, modified 2006]
 
 
EC 2.4.1.80     
Accepted name: ceramide glucosyltransferase
Reaction: UDP-α-D-glucose + an N-acylsphingosine = UDP + a β-D-glucosyl-N-acylsphingosine
For diagram of glycolipid biosynthesis, 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 β-D-glucosyltransferase (configuration-inverting)
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
For diagram of the biosynthesis of apigenin derivatives, click here and of luteolin derivatives, click here
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. [DOI] [PMID: 5058406]
[EC 2.4.1.81 created 1976]
 
 
EC 2.4.1.84      
Deleted entry:  UDP-glucuronate—1,2-diacylglycerol glucuronosyltransferase. Now included with EC 2.4.1.17, 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 of dhurrin biosynthesis, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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 lactotetraosylceramide biosynthesis, 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; UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase
Comments: The enzyme transfers galactose from UDP-α-D-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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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 α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→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-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-α-D-galactosaminyl-(1→3)-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 globotetraosylceramide biosynthesis, 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-glucosyl-(1↔1)-ceramide α-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 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. [DOI] [PMID: 4823436]
[EC 2.4.1.88 created 1976]
 
 
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. [DOI] [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. [DOI] [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
For diagram of kaempferol biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-glycoside derivatives, click here
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. [DOI] [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 ganglioside biosynthesis, click here
Glossary: ganglioside GM2 = 1-O-[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]-ceramideganglioside GM3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside GD3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide ganglioside GD2 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-[2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside SM3 = 1-O-[4-O-(3-O-sulfo-β-D-galactopyranosyl)-β-D-glucopyranosyl]-ceramideganglioside 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-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 1,4-β-N-acetyl-D-galactosaminyltransferase acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase; GM2/GD2-synthase; β-1,4N-acetylgalactosaminyltransferase; 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-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15710896]
[EC 2.4.1.92 created 1976, modified 2006]
 
 
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. [DOI] [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 2.4.1.96     
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. [DOI] [PMID: 11946194]
[EC 2.4.1.96 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 2.4.1.101     
Accepted name: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Glossary: Man5GlcNAc2-[protein] = α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Man5GlcNAc3-[protein]= β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Other name(s): MGAT1 (gene name); N-acetylglucosaminyltransferase I; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; uridine diphosphoacetylglucosamine-α-1,3-mannosylglycoprotein β-1,2-N-acetylglucosaminyltransferase; UDP-N-acetylglucosaminyl:α-1,3-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I; UDP-N-acetylglucosaminyl:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I; α-1,3-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTI; GlcNAc-T I; UDP-N-acetyl-D-glucosamine:3-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→3)-β-D-Man-R.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102576-81-8
References:
1.  Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358]
2.  Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163]
3.  Oppenheimer, C.L. and Hill, R.L. Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799–804. [PMID: 6450208]
4.  Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827]
5.  Miyagi, T. and Tsuiki, S. Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas. Biochim. Biophys. Acta 661 (1981) 148–157. [DOI] [PMID: 6170335]
6.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
7.  Vella, G.J., Paulsen, H. and Schachter, H. Control of glycoprotein synthesis. IX. A terminal Man alphal-3Man β1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: α-D-mannoside (GlcNAc to Man α1-3) β2-N-acetylglucosaminyltransferase I. Can. J. Biochem. Cell Biol. 62 (1984) 409–417. [PMID: 6235906]
8.  Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 19 (2000) 5269–5280. [DOI] [PMID: 11032794]
[EC 2.4.1.101 created 1983, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.102     
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Glossary: core 1 = O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein]
core 2 = O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(1→6)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase; GCNT1; GCNT3; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R) 6-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 1 structure of O-glycans forming core 2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
2.  Williams, D., Longmore, G., Matta, K.L. and Schachter, H. Mucin synthesis. II. Substrate specificity and product identification studies on canine submaxillary gland UDP-GlcNAc:Gal β1-3GalNAc(GlcNAc→GalNAc) β6-N-acetylglucosaminyltransferase. J. Biol. Chem. 255 (1980) 11253–11261. [PMID: 6449508]
3.  Williams, D. and Schachter, H. Mucin synthesis. I. Detection in canine submaxillary glands of an N-acetylglucosaminyltransferase which acts on mucin substrates. J. Biol. Chem. 255 (1980) 11247–11252. [PMID: 6449507]
[EC 2.4.1.102 created 1983, modified 2018]
 
 
EC 2.4.1.103     
Accepted name: alizarin 2-β-glucosyltransferase
Reaction: UDP-glucose + 1,2-dihydroxy-9,10-anthraquinone = UDP + 1-hydroxy-2-(β-D-glucosyloxy)-9,10-anthraquinone
Glossary: alizarin = 1,2-dihydroxy-9,10-anthraquinone
Other name(s): uridine diphosphoglucose-alizarin glucosyltransferase
Systematic name: UDP-glucose:1,2-dihydroxy-9,10-anthraquinone 2-O-β-D-glucosyltransferase
Comments: Acts on other hydroxy- and dihydroxy-derivatives of 9,10-anthraquinone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74506-41-5
References:
1.  Mateju, J., Cudlin, J., Steinerova, N., Blumauerova, M. and Vanek, Z. Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens. Folia Microbiol. 24 (1979) 205–210. [PMID: 38193]
[EC 2.4.1.103 created 1983]
 
 
EC 2.4.1.104     
Accepted name: o-dihydroxycoumarin 7-O-glucosyltransferase
Reaction: UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin
Other name(s): uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase
Systematic name: UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase
Comments: Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74114-37-7
References:
1.  Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177–184.
[EC 2.4.1.104 created 1983]
 
 
EC 2.4.1.105     
Accepted name: vitexin β-glucosyltransferase
Reaction: UDP-glucose + vitexin = UDP + vitexin 2′′-O-β-D-glucoside
For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here
Other name(s): uridine diphosphoglucose-vitexin 2′′-glucosyltransferase
Systematic name: UDP-glucose:vitexin 2′′-O-β-D-glucosyltransferase
Comments: Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76828-68-7
References:
1.  Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.
[EC 2.4.1.105 created 1983]
 
 
EC 2.4.1.106     
Accepted name: isovitexin β-glucosyltransferase
Reaction: UDP-glucose + isovitexin = UDP + isovitexin 2′′-O-β-D-glucoside
For diagram of the biosynthesis of vitexin and isovitexin derivatives, click here
Other name(s): uridine diphosphoglucose-isovitexin 2′′-glucosyltransferase
Systematic name: UDP-glucose:isovitexin 2′′-O-β-D-glucosyltransferase
Comments: Isovitexin is a flavonoid from petals of Silene alba.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72102-99-9
References:
1.  Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2′′-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935–1937.
[EC 2.4.1.106 created 1983]
 
 
EC 2.4.1.107      
Deleted entry:  UDP-glucuronate—testosterone glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.107 created 1983, deleted 1984]
 
 
EC 2.4.1.108      
Deleted entry:  UDP-glucuronate—phenol glucuronosyltransferase. Now included with EC 2.4.1.17, glucuronosyltransferase
[EC 2.4.1.108 created 1983, deleted 1984]
 
 
EC 2.4.1.111     
Accepted name: coniferyl-alcohol glucosyltransferase
Reaction: UDP-glucose + coniferyl alcohol = UDP + coniferin
Other name(s): uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase
Systematic name: UDP-glucose:coniferyl-alcohol 4′-β-D-glucosyltransferase
Comments: Sinapyl alcohol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61116-23-2
References:
1.  Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700–708. [DOI] [PMID: 10853]
[EC 2.4.1.111 created 1984]
 
 
EC 2.4.1.112      
Deleted entry: α-1,4-glucan-protein synthase (UDP-forming). The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase
[EC 2.4.1.112 created 1984, deleted 2007]
 
 
EC 2.4.1.114     
Accepted name: 2-coumarate O-β-glucosyltransferase
Reaction: UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-β-D-glucosyl-2-hydroxycinnamate
Other name(s): uridine diphosphoglucose-o-coumarate glucosyltransferase; UDPG:o-coumaric acid O-glucosyltransferase
Systematic name: UDP-glucose:trans-2-hydroxycinnamate O-β-D-glucosyltransferase
Comments: Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73665-97-1
References:
1.  Kleinhofs, A., Haskins, F.A. and Gorz, H.J. trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of Melilotus alba. Phytochemistry 6 (1967) 1313–1318.
2.  Poulton, J.E., McRee, B.E. and Conn, E.E. Intracellular localization of two enzymes involved in coumarin biosynthesis in Melilotus alba. Plant Physiol. 65 (1980) 171–175. [PMID: 16661155]
[EC 2.4.1.114 created 1984]
 
 
EC 2.4.1.115     
Accepted name: anthocyanidin 3-O-glucosyltransferase
Reaction: UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside
For diagram of anthocyanin biosynthesis, click here
Other name(s): uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT
Systematic name: UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase
Comments: The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, anthocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65607-32-1
References:
1.  Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045–1058. [PMID: 751640]
2.  Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224–9233. [DOI] [PMID: 9535914]
3.  Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797–25803. [DOI] [PMID: 11316805]
[EC 2.4.1.115 created 1984 (EC 2.4.1.233 created 2004, incorporated 2005), modified 2005]
 
 
EC 2.4.1.116     
Accepted name: cyanidin 3-O-rutinoside 5-O-glucosyltransferase
Reaction: UDP-α-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside
For diagram of anthocyanidin rutoside biosynthesis, click here
Glossary: cyanidin 3-O-rutinoside = cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase
Comments: Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 70248-66-7
References:
1.  Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
2.  Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino I. Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162 (2002) 779–784.
3.  Imayama, T., Yoshihara, Y., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167 (2004) 1243–1248.
[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006, modified 2013]
 
 
EC 2.4.1.117     
Accepted name: dolichyl-phosphate β-glucosyltransferase
Reaction: UDP-α-D-glucose + dolichyl phosphate = UDP + dolichyl β-D-glucosyl phosphate
Other name(s): polyprenyl phosphate:UDP-D-glucose glucosyltransferase; UDP-glucose dolichyl-phosphate glucosyltransferase; uridine diphosphoglucose-dolichol glucosyltransferase; UDP-glucose:dolichol phosphate glucosyltransferase; UDP-glucose:dolicholphosphoryl glucosyltransferase; UDP-glucose:dolichyl monophosphate glucosyltransferase; UDP-glucose:dolichyl phosphate glucosyltransferase; UDP-glucose:dolichyl-phosphate β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:dolichyl-phosphate β-D-glucosyltransferase (configuration-inverting)
Comments: Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 71061-42-2
References:
1.  Behrens, N.H. and Leloir, L.F. Dolichol monophosphate glucose: an intermediate in glucose transfer in liver. Proc. Natl. Acad. Sci. USA 66 (1970) 153–159. [DOI] [PMID: 5273893]
2.  Herscovics, A., Bugge, B. and Jeanloz, R.W. Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J. Biol. Chem. 252 (1977) 2271–2277. [PMID: 849929]
3.  Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase. J. Biol. Chem. 254 (1979) 4814–4819. [PMID: 438216]
[EC 2.4.1.117 created 1984]
 
 


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