The Enzyme Database

Displaying entries 51-100 of 2074.

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EC 2.4.1.288     Relevance: 100%
Accepted name: galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase
Reaction: 28 UDP-α-D-galactofuranose + β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol = 28 UDP + [β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→6)]14-β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of arabinofuranogalactofuranan biosynthesis, click here
Other name(s): GlfT2
Systematic name: UDP-α-D-galactofuranose:β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-β/5-β-D-galactofuranosyltransferase
Comments: Isolated from Mycobacterium tuberculosis. The enzyme adds approximately twenty-eight galactofuranosyl residues with alternating 1→5 and 1→6 links forming a galactan domain with approximately thirty galactofuranosyl residues. Involved in the formation of the cell wall in mycobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rose, N.L., Zheng, R.B., Pearcey, J., Zhou, R., Completo, G.C. and Lowary, T.L. Development of a coupled spectrophotometric assay for GlfT2, a bifunctional mycobacterial galactofuranosyltransferase. Carbohydr. Res. 343 (2008) 2130–2139. [DOI] [PMID: 18423586]
2.  May, J.F., Splain, R.A., Brotschi, C. and Kiessling, L.L. A tethering mechanism for length control in a processive carbohydrate polymerization. Proc. Natl. Acad. Sci. USA 106 (2009) 11851–11856. [DOI] [PMID: 19571009]
3.  Wheatley, R.W., Zheng, R.B., Richards, M.R., Lowary, T.L. and Ng, K.K. Tetrameric structure of the GlfT2 galactofuranosyltransferase reveals a scaffold for the assembly of mycobacterial Arabinogalactan. J. Biol. Chem. 287 (2012) 28132–28143. [DOI] [PMID: 22707726]
[EC 2.4.1.288 created 2012]
 
 
EC 2.4.1.206     Relevance: 99.5%
Accepted name: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of lactotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): LA2 synthase; β1→3-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lactosylceramide β-acetylglucosaminyltransferase; lactosylceramide β-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-β-D-glucosylceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-80-8
References:
1.  Gottfries, J., Percy, A.K., Maansson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253–261. [DOI] [PMID: 1825612]
2.  Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1→3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649–15658. [PMID: 2960671]
3.  Percy, A.K., Gottfries, J., Vilbergsson, G., Maansson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461–1465. [DOI] [PMID: 1901591]
[EC 2.4.1.206 created 1992]
 
 
EC 2.7.8.45     Relevance: 98.8%
Accepted name: teichoic acid glycerol-phosphate transferase
Reaction: CDP-glycerol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CDP + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): tarF (gene name) (ambiguous); teichoic acid glycerol-phosphate primase
Systematic name: CDP-glycerol:4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell walls of some bacteria such as Staphylococcus aureus. This enzyme adds a second glycerol unit to the disaccharide linker of the teichoic acid. cf. EC 2.7.8.12, teichoic acid poly(glycerol phosphate) polymerase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12–21. [DOI] [PMID: 18215769]
2.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.45 created 2017]
 
 
EC 2.4.1.65     Relevance: 98.8%
Accepted name: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-β-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-β-D-glucosaminyl-R 4I-α-L-fucosyltransferase (configuration-inverting)
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. [DOI] [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. [DOI] [PMID: 12676935]
[EC 2.4.1.65 created 1972, modified 2001, modified twice 2002]
 
 
EC 2.7.8.47     Relevance: 98.3%
Accepted name: teichoic acid ribitol-phosphate polymerase
Reaction: n CDP-ribitol + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 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
Other name(s): Tar polymerase (ambiguous); tarL (gene name) (ambiguous)
Systematic name: CDP-ribitol:4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the 25-35 ribitol units to the linker molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.47 created 2017]
 
 
EC 5.1.3.26     Relevance: 95.9%
Accepted name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
Reaction: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): GlcNAc-P-P-Und epimerase; GlcNAc-P-P-Und 4-epimerase; gne (gene name)
Systematic name: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
Comments: The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rush, J.S., Alaimo, C., Robbiani, R., Wacker, M. and Waechter, C.J. A novel epimerase that converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157. J. Biol. Chem. 285 (2010) 1671–1680. [DOI] [PMID: 19923219]
[EC 5.1.3.26 created 2013]
 
 
EC 2.4.1.305     Relevance: 95.7%
Accepted name: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase
Reaction: UDP-α-D-glucose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Glc-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfaP; WfgD; UDP-Glc:GlcNAc-pyrophosphate-lipid β-1,3-glucosyltransferase; UDP-Glc:GlcNAc-diphosphate-lipid β-1,3-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,3-glucosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brockhausen, I., Hu, B., Liu, B., Lau, K., Szarek, W.A., Wang, L. and Feng, L. Characterization of two β-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152. J. Bacteriol. 190 (2008) 4922–4932. [DOI] [PMID: 18487334]
[EC 2.4.1.305 created 2013]
 
 
EC 2.4.1.52     Relevance: 95.6%
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, PDB, 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 2.4.1.129      
Transferred entry: peptidoglycan glycosyltransferase. Now EC 2.4.99.28, peptidoglycan glycosyltransferase
[EC 2.4.1.129 created 1984, modified 2002, deleted 2023]
 
 
EC 2.4.99.28     Relevance: 95.5%
Accepted name: peptidoglycan glycosyltransferase
Reaction: [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
Glossary: Mur2Ac = N-acetylmuramic acid
Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
Systematic name: [poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2
References:
1.  Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [DOI] [PMID: 6802846]
2.  Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [DOI] [PMID: 9841666]
3.  van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055]
[EC 2.4.99.28 created 1984 as EC 2.4.1.129, modified 2002, transferred 2023 to EC 2.4.99.28]
 
 
EC 3.2.1.169     Relevance: 95%
Accepted name: protein O-GlcNAcase
Reaction: (1) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine
(2) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-theronine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine
Other name(s): OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase
Systematic name: [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase
Comments: Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gao, Y., Wells, L., Comer, F.I., Parker, G.J. and Hart, G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276 (2001) 9838–9845. [DOI] [PMID: 11148210]
2.  Wells, L., Gao, Y., Mahoney, J.A., Vosseller, K., Chen, C., Rosen, A. and Hart, G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase. J. Biol. Chem. 277 (2002) 1755–1761. [PMID: 11788610]
3.  Cetinbas, N., Macauley, M.S., Stubbs, K.A., Drapala, R. and Vocadlo, D.J. Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 45 (2006) 3835–3844. [DOI] [PMID: 16533067]
4.  Dennis, R.J., Taylor, E.J., Macauley, M.S., Stubbs, K.A., Turkenburg, J.P., Hart, S.J., Black, G.N., Vocadlo, D.J. and Davies, G.J. Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity. Nat. Struct. Mol. Biol. 13 (2006) 365–371. [DOI] [PMID: 16565725]
5.  Kim, E.J., Kang, D.O., Love, D.C. and Hanover, J.A. Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate. Carbohydr. Res. 341 (2006) 971–982. [DOI] [PMID: 16584714]
6.  Dong, D.L. and Hart, G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269 (1994) 19321–19330. [PMID: 8034696]
[EC 3.2.1.169 created 2011]
 
 
EC 3.5.1.136     Relevance: 93.7%
Accepted name: N,N′-diacetylchitobiose non-reducing end deacetylase
Reaction: N,N′-diacetylchitobiose + H2O = β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine + acetate
Other name(s): diacetylchitobiose deacetylase (ambiguous); cda (gene name)
Systematic name: N,N′-diacetylchitobiose non-reducing end acetylhydrolase
Comments: The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N′-diacetylchitobiose, the end product of the archaeal chitinase, to produce β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N′-diacetylchitobiose at the reducing residue to produce N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H. and Imanaka, T. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279 (2004) 30021–30027. [DOI] [PMID: 15136574]
2.  Mine, S., Ikegami, T., Kawasaki, K., Nakamura, T. and Uegaki, K. Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii. Protein Expr. Purif. 84 (2012) 265–269. [DOI] [PMID: 22713621]
3.  Nakamura, T., Yonezawa, Y., Tsuchiya, Y., Niiyama, M., Ida, K., Oshima, M., Morita, J. and Uegaki, K. Substrate recognition of N,N′-diacetylchitobiose deacetylase from Pyrococcus horikoshii. J. Struct. Biol. 195:S1047-8477( (2016). [DOI] [PMID: 27456364]
[EC 3.5.1.136 created 2020]
 
 
EC 2.4.1.53     Relevance: 92.7%
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 2.7.8.33     Relevance: 92%
Accepted name: UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate
Other name(s): UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase; UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase; GlcNAc-P-P-Und synthase; GPT (ambiguous); TagO; UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetylglucosaminephosphotransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-α-D-glucosaminephosphotransferase
Comments: This enzyme catalyses the synthesis of N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J. Bacteriol. 190 (2008) 7141–7146. [DOI] [PMID: 18723618]
2.  Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide. J. Bacteriol. 189 (2007) 2618–2628. [DOI] [PMID: 17237164]
3.  Rush, J.S., Rick, P.D. and Waechter, C.J. Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli. Glycobiology 7 (1997) 315–322. [DOI] [PMID: 9134438]
4.  Soldo, B., Lazarevic, V. and Karamata, D. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 (2002) 2079–2087. [DOI] [PMID: 12101296]
[EC 2.7.8.33 created 2011]
 
 
EC 3.2.1.96     Relevance: 91.9%
Accepted name: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Reaction: Endohydrolysis of the N,N′-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
Other name(s): N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1→4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H
Systematic name: glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
Comments: A group of related enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-88-9
References:
1.  Chien, S., Weinburg, R., Li, S. and Li, Y. Endo-β-N-acetylglucosaminidase from fig latex. Biochem. Biophys. Res. Commun. 76 (1977) 317–323. [DOI] [PMID: 1027432]
2.  Koide, N. and Muramatsu, T. Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. Biol. Chem. 249 (1974) 4897–4904. [PMID: 4152561]
3.  Pierce, R.J., Spik, G. and Montreuil, J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180 (1979) 673. [PMID: 486141]
4.  Pierce, R.J., Spik, G. and Montreuil, J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185 (1980) 261–264. [PMID: 7378051]
5.  Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem. 250 (1975) 8569–8575. [PMID: 389]
6.  Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249 (1974) 818–824. [PMID: 4204553]
[EC 3.2.1.96 created 1978]
 
 
EC 2.4.1.69     Relevance: 91.3%
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 lactotetraosylceramide biosynthesis, 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, PDB, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 10589734]
[EC 2.4.1.69 created 1972 (EC 2.4.1.89 created 1976, incorporated 1984), modified 2002, modified 2017]
 
 
EC 3.1.4.45     Relevance: 90.8%
Accepted name: N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase
Reaction: glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
Other name(s): α-N-acetylglucosaminyl phosphodiesterase; lysosomal α-N-acetylglucosaminidase; phosphodiester glycosidase; α-N-acetyl-D-glucosamine-1-phosphodiester N-acetylglucosaminidase; 2-acetamido-2-deoxy-α-D-glucose 1-phosphodiester acetamidodeoxyglucohydrolase
Systematic name: glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase
Comments: Acts on a variety of compounds in which N-acetyl-D-glucosamine is α-linked to a phosphate group, including the biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the products of EC 2.7.8.17 UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75788-84-0
References:
1.  Van den Tweel, W.J.J., Smits, J.P., Ogg, R.L.H.P. and de Bont, J.A.M. The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida. Appl. Microbiol. Biotechnol. 29 (1988) 224–230.
2.  van der Drift, C., van Helvoort, P.E. and Vogels, G.D. S-Ureidoglycolate dehydrogenase: purification and properties. Arch. Biochem. Biophys. 145 (1971) 465–469. [DOI] [PMID: 4399430]
3.  van der Drift, L., Vogels, G.D. and van der Drift, C. Allantoin racemase: a new enzyme from Pseudomonas species. Biochim. Biophys. Acta 391 (1975) 240–248. [DOI] [PMID: 237557]
4.  Waheed, A., Hasilik, A. and von Figura, K. Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal α-N-acetylglucosaminyl phosphodiesterase. J. Biol. Chem. 256 (1981) 5717–5721. [PMID: 6263889]
[EC 3.1.4.45 created 1984]
 
 
EC 2.7.8.14     Relevance: 90.3%
Accepted name: CDP-ribitol ribitolphosphotransferase
Reaction: n CDP-ribitol + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 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
Other name(s): teichoic-acid synthase (ambiguous); polyribitol phosphate synthetase (ambiguous); teichoate synthetase (ambiguous); poly(ribitol phosphate) synthetase (ambiguous); polyribitol phosphate polymerase (ambiguous); teichoate synthase (ambiguous); CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase
Systematic name: CDP-ribitol:4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase
Comments: Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds around 40 ribitol units to the linker molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-71-5
References:
1.  Ishimoto, N. and Strominger, J.L. Polyribitol phosphate synthetase of Staphylococcus aureus. J. Biol. Chem. 241 (1966) 639–650. [PMID: 5908130]
2.  Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12–21. [DOI] [PMID: 18215769]
3.  Pereira, M.P., D'Elia, M.A., Troczynska, J. and Brown, E.D. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190 (2008) 5642–5649. [DOI] [PMID: 18556787]
4.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.14 created 1972 as EC 2.4.1.55, transferred 1982 to EC 2.7.8.14, modified 2017]
 
 
EC 2.4.1.386     Relevance: 90.1%
Accepted name: GlcNAc-β-1,3-Gal β-1,6-N-acetylglucosaminyltransferase (distally acting)
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Other name(s): UDP-GlcNAc:GlcNAcβ1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase; dIGnT; C2GnT2 (misleading)
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Involved in the production of milk oligosaccharides in the lacto-N-triose (LNT) series. Cf. EC 2.4.1.150 (N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase; cIGnT) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658]
2.  Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862]
[EC 2.4.1.386 created 2021]
 
 
EC 2.4.1.304     Relevance: 90%
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449–459. [DOI] [PMID: 21057010]
[EC 2.4.1.304 created 2013]
 
 
EC 2.4.1.94     Relevance: 89.6%
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 3.5.1.105     Relevance: 89.2%
Accepted name: chitin disaccharide deacetylase
Reaction: N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate
Glossary: N,N′-diacetylchitobiose = N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine
Other name(s): chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase; 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
Systematic name: N,N′-diacetylchitobiose acetylhydrolase
Comments: Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357–365. [DOI] [PMID: 17334758]
2.  Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046–1053. [DOI] [PMID: 19553519]
3.  Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113–1117.
4.  Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561–563. [DOI] [PMID: 16232910]
[EC 3.5.1.105 created 2010]
 
 
EC 3.5.1.89     Relevance: 87.2%
Accepted name: N-acetylglucosaminylphosphatidylinositol deacetylase
Reaction: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Other name(s): N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase
Systematic name: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase
Comments: Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122191-30-4
References:
1.  Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168–11173. [PMID: 2525555]
2.  Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834–15840. [DOI] [PMID: 9188481]
3.  Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185–192. [PMID: 10085243]
4.  Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322–3332. [DOI] [PMID: 11432820]
[EC 3.5.1.89 created 1992 as EC 3.1.1.69, transferred 2002 to EC 3.5.1.89, modified 2002]
 
 
EC 2.7.8.12     Relevance: 86.5%
Accepted name: teichoic acid poly(glycerol phosphate) polymerase
Reaction: n CDP-glycerol + 4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): teichoic-acid synthase; cytidine diphosphoglycerol glycerophosphotransferase; poly(glycerol phosphate) polymerase; teichoic acid glycerol transferase; glycerophosphate synthetase; CGPTase; CDP-glycerol glycerophosphotransferase (ambiguous); Tag polymerase; CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase; tagF (gene name); tarF (gene name) (ambiguous)
Systematic name: CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Comments: Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30–50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-71-5
References:
1.  Burger, M.M. and Glaser, L. The synthesis of teichoic acids. I. Polyglycerophosphate. J. Biol. Chem. 239 (1964) 3168–3177. [PMID: 14245357]
2.  Schertzer, J.W. and Brown, E.D. Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro. J. Biol. Chem. 278 (2003) 18002–18007. [DOI] [PMID: 12637499]
3.  Schertzer, J.W., Bhavsar, A.P. and Brown, E.D. Two conserved histidine residues are critical to the function of the TagF-like family of enzymes. J. Biol. Chem. 280 (2005) 36683–36690. [DOI] [PMID: 16141206]
4.  Pereira, M.P., Schertzer, J.W., D'Elia, M.A., Koteva, K.P., Hughes, D.W., Wright, G.D. and Brown, E.D. The wall teichoic acid polymerase TagF efficiently synthesizes poly(glycerol phosphate) on the TagB product lipid III. ChemBioChem 9 (2008) 1385–1390. [DOI] [PMID: 18465758]
5.  Sewell, E.W., Pereira, M.P. and Brown, E.D. The wall teichoic acid polymerase TagF is non-processive in vitro and amenable to study using steady state kinetic analysis. J. Biol. Chem. 284 (2009) 21132–21138. [DOI] [PMID: 19520862]
6.  Lovering, A.L., Lin, L.Y., Sewell, E.W., Spreter, T., Brown, E.D. and Strynadka, N.C. Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis. Nat. Struct. Mol. Biol. 17 (2010) 582–589. [DOI] [PMID: 20400947]
7.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.12 created 1972, modified 1982, modified 2017]
 
 
EC 2.4.1.343     Relevance: 86.2%
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): wclR (gene name)
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-galactosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3. Requires a divalent metal ion (Mn2+, Mg2+ or Fe2+). cf. EC 2.4.1.303, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, C., Liu, B., Xu, Y., Utkina, N., Zhou, D., Danilov, L., Torgov, V., Veselovsky, V. and Feng, L. Biochemical characterization of the novel α-1, 3-galactosyltransferase WclR from Escherichia coli O3. Carbohydr. Res. 430 (2016) 36–43. [DOI] [PMID: 27196310]
[EC 2.4.1.343 created 2017]
 
 
EC 2.4.1.229     Relevance: 85.5%
Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline
Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase
Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 256531-81-4
References:
1.  van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [DOI] [PMID: 12244115]
2.  Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [DOI] [PMID: 10593934]
3.  West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [DOI] [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 
EC 2.4.1.280     Relevance: 85.4%
Accepted name: N,N′-diacetylchitobiose phosphorylase
Reaction: N,N′-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-α-D-glucosamine 1-phosphate
Glossary: N,N′-diacetylchitobiose = N-acetyl-D-glucosaminyl-β-(1→4)-N-acetyl-D-glucosamine
Other name(s): chbP (gene name)
Systematic name: N,N′-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase
Comments: The enzyme is specific for N,N′-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Park, J.K., Keyhani, N.O. and Roseman, S. Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275 (2000) 33077–33083. [DOI] [PMID: 10913116]
2.  Honda, Y., Kitaoka, M. and Hayashi, K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem. J. 377 (2004) 225–232. [DOI] [PMID: 13678418]
3.  Hidaka, M., Honda, Y., Kitaoka, M., Nirasawa, S., Hayashi, K., Wakagi, T., Shoun, H. and Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold. Structure 12 (2004) 937–947. [DOI] [PMID: 15274915]
[EC 2.4.1.280 created 2012]
 
 
EC 2.4.1.147     Relevance: 85%
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] = UDP + O3-[N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein]
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase; mucin core 3 β3-GlcNAc-transferase; Core 3β-GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase (incorrect)
Systematic name: UDP-N-acetyl-α-D-glucosamine:O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase
Comments: The product of the enzyme is known as core 3, one of the eight core structures of mucin-type O-glycans. O-Linked glycans are polysaccharides or oligosaccharides that are linked to a protein via the oxygen atom in the side chain of an L-serine or L-threonine residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87927-96-6
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.  Brockhausen, I., Matta, K.L., Orr, J. and Schachter, H. Mucin synthesis. UDP-GlcNAc:GalNAc-R β 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc β 1-3GalNAc-R (GlcNAc to GalNAc) β 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa. Biochemistry 24 (1985) 1866–1874. [PMID: 3160388]
3.  Vavasseur, F., Yang, J.M., Dole, K., Paulsen, H. and Brockhausen, I. Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R β 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal tissues and lack of the activity in human cancer cell lines. Glycobiology 5 (1995) 351–357. [DOI] [PMID: 7655172]
[EC 2.4.1.147 created 1984, modified 2015]
 
 
EC 2.4.1.312     Relevance: 84.6%
Accepted name: protein O-mannose β-1,4-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 3-O-(α-D-mannosyl)-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]
For diagram of glycoprotein biosynthesis, click here
Other name(s): GTDC2 (gene name); POMGNT2
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-threonyl-[protein] 4-β-N-acetyl-D-glucosaminyltransferase
Comments: The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]
[EC 2.4.1.312 created 2013]
 
 
EC 2.7.8.15     Relevance: 84.5%
Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase; uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase; chitobiosylpyrophosphoryldolichol synthase; dolichol phosphate N-acetylglucosamine-1-phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase
Systematic name: UDP-N-α-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase (configuration-retaining)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70431-08-2
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245]
2.  Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem. 255 (1980) 8174–8178. [PMID: 6447695]
[EC 2.7.8.15 created 1983]
 
 
EC 2.4.1.303     Relevance: 84.3%
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn2+. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605–613. [DOI] [PMID: 15625181]
2.  Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663–673. [DOI] [PMID: 18536883]
[EC 2.4.1.303 created 2013, modified 2017]
 
 
EC 2.4.1.38     Relevance: 82.6%
Accepted name: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide
Other name(s): UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase
Comments: Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-43-7
References:
1.  Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450]
2.  Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [DOI] [PMID: 6816588]
3.  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]
4.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898]
[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986]
 
 
EC 2.4.1.344     Relevance: 82.3%
Accepted name: type 2 galactoside α-(1,2)-fucosyltransferase
Reaction: GDP-β-L-fucose + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = GDP + α-L-fucosyl-(1→2)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): blood group H α-2-fucosyltransferase (ambiguous); guanosine diphosphofucose-galactoside 2-L-fucosyltransferase (ambiguous); 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-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; 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); H-gene-encoded β-galactoside α(1→2)fucosyltransferase; β-galactoside α(1→2)fucosyltransferase (ambiguous); GDP-L-fucose:lactose fucosyltransferase; GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase (ambiguous); FUT1 (gene name); FUT2 (gene name)
Systematic name: GDP-β-L-fucose:β-D-galactosyl-(1→4)-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 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956–2962. [PMID: 804484]
2.  Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351–353.
3.  Ernst, L.K., Rajan, V.P., Larsen, R.D., Ruff, M.M. and Lowe, J.B. Stable expression of blood group H determinants and GDP-L-fucose: β-D-galactoside 2-α-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264 (1989) 3436–3447. [PMID: 2464598]
4.  Larsen, R.D., Ernst, L.K., Nair, R.P. and Lowe, J.B. Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc. Natl. Acad. Sci. USA 87 (1990) 6674–6678. [DOI] [PMID: 2118655]
[EC 2.4.1.344 created 2017]
 
 
EC 2.4.1.222     Relevance: 79.2%
Accepted name: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) = UDP + [protein with EGF-like domain]-3-O-[N-acetyl-β-D-glucosaminyl-(1→3)-α-L-fucosyl]-(L-serine/L-threonine)
Glossary: EGF = epidermal growth factor
EGF-like domain = an evolutionary conserved domain containing 30 to 40 amino-acid residues first described from epidermal growth factor
Other name(s): O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase; fringe; UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc and α-Neu5Ac-(2→6)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 299203-70-6
References:
1.  Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369–375. [DOI] [PMID: 10935626]
2.  Bruckner, K., Perez, L., Clausen, H. and Cohen, S. Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406 (2000) 411–415. [DOI] [PMID: 10935637]
3.  Rampal, R., Li, A.S., Moloney, D.J., Georgiou, S.A., Luther, K.B., Nita-Lazar, A. and Haltiwanger, R.S. Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeats. J. Biol. Chem. 280 (2005) 42454–42463. [DOI] [PMID: 16221665]
[EC 2.4.1.222 created 2002, modified 2022]
 
 
EC 2.7.8.35     Relevance: 77.4%
Accepted name: UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + trans,octacis-decaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of galactofuranan biosynthesis, click here
Other name(s): GlcNAc-1-phosphate transferase; UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Comments: Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-α-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, Y., Xin, Y., Zhang, W. and Ma, Y. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol. Lett. 310 (2010) 54–61. [DOI] [PMID: 20637039]
[EC 2.7.8.35 created 2012]
 
 
EC 2.4.1.153     Relevance: 76.9%
Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UDP + dolichyl N-acetyl-α-D-glucosaminyl phosphate
Other name(s): aglK (gene name); dolichyl-phosphate α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-73-5
References:
1.  Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367–373. [DOI] [PMID: 23624439]
[EC 2.4.1.153 created 1984, modified 2015]
 
 
EC 2.4.1.267     Relevance: 74.9%
Accepted name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493–498. [DOI] [PMID: 8877369]
2.  Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412–417. [PMID: 6423630]
3.  Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420–421. [DOI] [PMID: 14517965]
[EC 2.4.1.267 created 2011, modified 2012]
 
 
EC 2.4.1.265     Relevance: 73%
Accepted name: dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977–5981. [DOI] [PMID: 8016100]
2.  Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582–15590. [PMID: 3536907]
3.  Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962–9971. [DOI] [PMID: 12480927]
[EC 2.4.1.265 created 2011, modified 2012]
 
 
EC 2.4.99.2      
Transferred entry: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.2, β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
[EC 2.4.99.2 created 1976, modified 1986, deleted 2022]
 
 
EC 2.4.3.2     Relevance: 72.7%
Accepted name: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R
For diagram of ganglioside biosynthesis, click here
Glossary: a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a
Other name(s): CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate: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 N-acetyl-β-neuraminyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-12-2
References:
1.  Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198]
2.  Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506]
[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2]
 
 
EC 2.4.99.7      
Transferred entry: α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase. Now EC 2.4.3.7, α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase
[EC 2.4.99.7 created 1984, modified 1986, modified 2004, deleted 2022]
 
 
EC 3.5.1.33     Relevance: 72.1%
Accepted name: N-acetylglucosamine deacetylase
Reaction: N-acetyl-D-glucosamine + H2O = D-glucosamine + acetate
Other name(s): acetylaminodeoxyglucose acetylhydrolase; N-acetyl-D-glucosaminyl N-deacetylase
Systematic name: N-acetyl-D-glucosamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-32-2
References:
1.  Roseman, S. Glucosamine metabolism. I. N-Acetylglucosamine deacetylase. J. Biol. Chem. 226 (1957) 115–123. [PMID: 13428742]
[EC 3.5.1.33 created 1972]
 
 
EC 2.4.3.7     Relevance: 71.3%
Accepted name: α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase
Reaction: CMP-N-acetylneuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-D-galactosaminyl-R
For diagram of reaction, click here
Other name(s): sialyltransferase; cytidine monophosphoacetylneuraminate-(α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetylgalactosaminide-α-2,6-sialyltransferase; α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetyl-galactosaminide α-2,6-sialyltransferase; SIAT7; ST6GALNAC; (α-N-acetylneuraminyl-2,3-β-galactosyl-1,3)-N-acetyl-galactosaminide 6-α-sialyltransferase; CMP-N-acetylneuraminate:(α-N-acetylneuraminyl-2,3-β-D-galactosyl-1,3)-N-acetyl-D-galactosaminide α-2,6-N-acetylneuraminyl-transferase
Systematic name: CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)- N-acetyl-D-galactosaminide galactosamine-6-α-N-acetylneuraminyltransferase
Comments: Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetylgalactosamine only when present in the structure of α-N-acetylneuraminyl-(2→3)-β-galactosyl-(1→3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol. Not identical with EC 2.4.3.3 α-N-acetylgalactosaminide α-2,6-sialyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129924-24-9
References:
1.  Bergh, M.L.E., Hooghwinkel, G.J.M. and Van den Eijnden, D.H. Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an α-N-acetylgalactosaminide α2→6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. J. Biol. Chem. 258 (1983) 7430–7436. [PMID: 6190802]
[EC 2.4.3.7 created 1984 as EC 2.4.99.7, modified 1986, modified 2004, transferred 2022 to EC 2.4.3.7]
 
 
EC 2.4.1.132     Relevance: 71.2%
Accepted name: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
Reaction: GDP-α-D-mannose + β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = β-D-mannosyl-(1→4)-N,N′-diacetylchitobiosyldiphosphodolichol
Other name(s): Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase
Systematic name: GDP-α-D-mannose:β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81181-76-2
References:
1.  Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
[EC 2.4.1.132 created 1984, modified 2011, modified 2012]
 
 
EC 2.4.1.256     Relevance: 70.9%
Accepted name: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining)
Comments: This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455–462. [DOI] [PMID: 9597543]
[EC 2.4.1.256 created 2011, modified 2012]
 
 
EC 2.4.1.88     Relevance: 69.3%
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 2.4.1.257     Relevance: 69.1%
Accepted name: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase
Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
[EC 2.4.1.257 created 2011, modified 2012]
 
 
EC 2.4.1.260     Relevance: 69%
Accepted name: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
2.  Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792–3802. [DOI] [PMID: 20023196]
3.  Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749–762. [PMID: 12460943]
4.  Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331–2339. [DOI] [PMID: 12217961]
[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012]
 
 
EC 2.4.1.261     Relevance: 66.7%
Accepted name: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [PMID: 19451548]
2.  Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012]
 
 
EC 2.4.3.1     Relevance: 66.7%
Accepted name: β-galactoside α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R
Other name(s): ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-81-4
References:
1.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897]
2.  Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609]
3.  Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915]
4.  Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932]
5.  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]
6.  Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092]
[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1]
 
 


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