The Enzyme Database

Displaying entries 1-50 of 1537.

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EC 2.4.1.341     Relevance: 100%
Accepted name: α-1,2-colitosyltransferase
Reaction: GDP-β-L-colitose + β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = GDP + α-L-colitosyl-(1→2)-β-D-galactosyl-(1→3)-N-acetyl-D-glucosamine
Glossary: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine = lacto-N-biose
Other name(s): wbgN (gene name)
Systematic name: GDP-β-L-colitose:β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine L-colitosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen. The reaction involves anomeric inversion, and does not require any metal ions. The enzyme is highly specific towards the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-β-L-colitose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wu, Z., Zhao, G., Li, T., Qu, J., Guan, W., Wang, J., Ma, C., Li, X., Zhao, W., Wang, P.G. and Li, L. Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7. Glycobiology (2015) . [DOI] [PMID: 26703456]
[EC 2.4.1.341 created 2016]
 
 
EC 2.4.1.211     Relevance: 97.3%
Accepted name: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase
Reaction: β-D-galactopyranosyl-(1→3)-N-acetyl-D-glucosamine + phosphate = α-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
Other name(s): lacto-N-biose phosphorylase; LNBP; galacto-N-biose phosphorylase
Systematic name: β-D-galactopyranosyl-(1→3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
Comments: Reaction also occurs with β-D-galactopyranosyl-(1→3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 224427-06-9
References:
1.  Derensy-Dron, D., Krzewinski, F., Brassart, C. and Bouquelet S. β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation. Biotechnol. Appl. Biochem. 29 (1999) 3–10. [PMID: 9889079]
[EC 2.4.1.211 created 2001]
 
 
EC 2.4.1.92     Relevance: 79.3%
Accepted name: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide = UDP + O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Glossary: ganglioside GM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-[N-acetyl-α-neuraminyl-(2→3)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside GM3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside GD3 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide ganglioside GD2 = 1-O-[O-(N-acetyl-α-neuraminyl)-(2→8)-O-(N-acetyl-α-neuraminyl)-(2→3)-O-[2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)]-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramideganglioside SM3 = 1-O-[4-O-(3-O-sulfo-β-D-galactopyranosyl)-β-D-glucopyranosyl]-ceramideganglioside SM2 = 1-O-[O-2-(acetylamino)-2-deoxy-β-D-galactopyranosyl-(1→4)-O-3-O-sulfo-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide
Other name(s): uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase; ganglioside GM2 synthase; ganglioside GM3 acetylgalactosaminyltransferase; GM2 synthase; UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 1,4-β-N-acetyl-D-galactosaminyltransferase acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase; GM2/GD2-synthase; β-1,4N-acetylgalactosaminyltransferase; asialo-GM2 synthase; GalNAc-T; UDP-N-acetyl-D-galactosamine:(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:1-O-[O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl]-ceramide 4-β-N-acetyl-D-galactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:O-(N-acetyl-α-neuraminyl)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyl-(1↔1)-ceramide 4-β-N-acetyl-D-galactosaminyltransferase
Comments: This enzyme catalyses the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively. Asialo-GM3 [3] and lactosylceramide [2] are also substrates, but glycoproteins and oligosaccharides are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67338-98-1
References:
1.  Dicesare, J.L. and Dain, J.A. The enzymic synthesis of ganglioside. IV. UDP-N-acetylgalactosamine: (N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyltransferase in rat brain. Biochim. Biophys. Acta 231 (1971) 385–393. [DOI] [PMID: 5554906]
2.  Pohlentz, G., Klein, D., Schwarzmann, G., Schmitz, D. and Sandhoff, K. Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proc. Natl. Acad. Sci. USA 85 (1988) 7044–7048. [DOI] [PMID: 3140234]
3.  Kazuya, I.-P., Hidari, J.K., Ichikawa, S., Furukawa, K., Yamasaki, M. and Hirabayashi, Y. β1-4N-Acetylgalactosaminyltransferase can synthesize both asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo: isolation and characterization of a β1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell line AH7974F. Biochem. J. 303 (1994) 957–965. [PMID: 7980468]
4.  Hashimoto, Y., Sekine, M., Iwasaki, K. and Suzuki, A. Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver. J. Biol. Chem. 268 (1993) 25857–25864. [PMID: 8245020]
5.  Nagai, K. and Ishizuka, I. Biosynthesis of monosulfogangliotriaosylceramide and GM2 by N-acetylgalactosaminyltransferase from rat brain. J. Biochem. (Tokyo) 101 (1987) 1115–1127. [PMID: 3115968]
6.  Furukawa, K., Takamiya, K. and Furukawa, K. β1,4-N-Acetylgalactosaminyltransferase—GM2/GD2 synthase: a key enzyme to control the synthesis of brain-enriched complex gangliosides. Biochim. Biophys. Acta 1573 (2002) 356–362. [DOI] [PMID: 12417418]
7.  Yamashita, T., Wu, Y.P., Sandhoff, R., Werth, N., Mizukami, H., Ellis, J.M., Dupree, J.L., Geyer, R., Sandhoff, K. and Proia, R.L. Interruption of ganglioside synthesis produces central nervous system degeneration and altered axon-glial interactions. Proc. Natl. Acad. Sci. USA 102 (2005) 2725–2730. [DOI] [PMID: 15710896]
[EC 2.4.1.92 created 1976, modified 2006]
 
 
EC 2.4.1.149     Relevance: 72%
Accepted name: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R
Other name(s): uridine diphosphoacetylglucosamine-acetyllactosaminide β1→3-acetylglucosaminyltransferase; poly-N-acetyllactosamine extension enzyme; Galβ1→4GlcNAc-R β1→3 N-acetylglucosaminyltransferase; UDP-GlcNAc:GalR β-D-3-N-acetylglucosaminyltransferase; N-acetyllactosamine β(1-3)N-acetylglucosaminyltransferase; UDP-GlcNAc:Galβ1→4GlcNAcβ-Rβ1→3-N-acetylglucosaminyltransferase; GnTE; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosamine β-1,3-acetyl-D-glucosaminyltransferase; β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine 3-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-R 3-β N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on glycoproteins, glycolipids, and oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85638-39-7
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  Takeya, A., Hosomi, O. and Kogure, T. The presence of N-acetyllactosamine and lactose: β (1-3)N-acetylglucosaminyltransferase activity in human urine. Jpn. J. Med. Sci. Biol. 38 (1985) 1–8. [PMID: 3160874]
[EC 2.4.1.149 created 1984 (EC 2.4.1.163 created 1989, incorporated 2016), modified 2016]
 
 
EC 2.4.1.164      
Transferred entry: galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,6-N-acetylglucosaminyltransferase, now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
[EC 2.4.1.164 created 1989, deleted 2016]
 
 
EC 2.4.1.163      
Transferred entry: β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase, now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
[EC 2.4.1.163 created 1989, deleted 2016]
 
 
EC 2.4.1.16     Relevance: 68%
Accepted name: chitin synthase
Reaction: UDP-N-acetyl-α-D-glucosamine + [(1→4)-N-acetyl-β-D-glucosaminyl]n = UDP + [(1→4)-N-acetyl-β-D-glucosaminyl]n+1
Glossary: chitin = [(1→4)-N-acetyl-β-D-glucosaminyl]n
Other name(s): chitin-UDP N-acetylglucosaminyltransferase; chitin-uridine diphosphate acetylglucosaminyltransferase; chitin synthetase; trans-N-acetylglucosaminosylase; UDP-N-acetyl-D-glucosamine:chitin 4-β-N-acetylglucosaminyl-transferase; UDP-N-acetyl-α-D-glucosamine:chitin 4-β-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:chitin 4-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Converts UDP-N-acetyl-α-D-glucosamine into chitin and UDP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-18-6
References:
1.  Glaser, L. and Brown, D.H. The synthesis of chitin in cell-free extracts of Neurospora crassa. J. Biol. Chem. 228 (1957) 729–742. [PMID: 13475355]
2.  Sburlati, A. and Cabib, E. Chitin synthetase 2, a presumptive participant in septum formation in Saccharomyces cerevisiae. J. Biol. Chem. 261 (1986) 15147–15152. [PMID: 2945823]
[EC 2.4.1.16 created 1961]
 
 
EC 2.4.1.146     Relevance: 67.4%
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] = UDP + 3-O-{N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Glossary: core 2 = 3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase (elongating); elongation 3β-GalNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to β-D-galactose of β-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→3)-[N-acetyl-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase; B3GNT3 (gene name)
Systematic name: UDP-N-acetyl-α-D-glucosamine:3-O-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 2 structure of O-glycans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87927-99-9
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.  Shiraishi, N., Natsume, A., Togayachi, A., Endo, T., Akashima, T., Yamada, Y., Imai, N., Nakagawa, S., Koizumi, S., Sekine, S., Narimatsu, H. and Sasaki, K. Identification and characterization of three novel β 1,3-N-acetylglucosaminyltransferases structurally related to the β 1,3-galactosyltransferase family. J. Biol. Chem. 276 (2001) 3498–3507. [PMID: 11042166]
[EC 2.4.1.146 created 1984, modified 2018]
 
 
EC 2.4.1.206     Relevance: 67%
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 2.4.1.102     Relevance: 65.4%
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Glossary: core 1 = O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein]
core 2 = O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein]
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(1→6)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase; GCNT1; GCNT3; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R) 6-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 1 structure of O-glycans forming core 2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
2.  Williams, D., Longmore, G., Matta, K.L. and Schachter, H. Mucin synthesis. II. Substrate specificity and product identification studies on canine submaxillary gland UDP-GlcNAc:Gal β1-3GalNAc(GlcNAc→GalNAc) β6-N-acetylglucosaminyltransferase. J. Biol. Chem. 255 (1980) 11253–11261. [PMID: 6449508]
3.  Williams, D. and Schachter, H. Mucin synthesis. I. Detection in canine submaxillary glands of an N-acetylglucosaminyltransferase which acts on mucin substrates. J. Biol. Chem. 255 (1980) 11247–11252. [PMID: 6449507]
[EC 2.4.1.102 created 1983, modified 2018]
 
 
EC 2.4.1.150     Relevance: 65.3%
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Glossary: β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = type 2 precursor disaccharide
Other name(s): GCNT2 (gene name); GCNT3 (gene name); IGnT; I-branching β1,6-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: The enzyme acts on poly-N-acetyllactosamine [glycan chains of β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine units connected by β(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by β(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  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]
4.  Bierhuizen, M.F., Maemura, K., Kudo, S. and Fukuda, M. Genomic organization of core 2 and I branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology 5 (1995) 417–425. [DOI] [PMID: 7579796]
5.  Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274 (1999) 9296–9304. [DOI] [PMID: 10092606]
6.  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 2.4.1.150 created 1984 (EC 2.4.1.164 created 1989, incorporated 2016), modified 2017]
 
 
EC 2.4.1.148     Relevance: 62.2%
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→3)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-mucin β(1→6)-acetylglucosaminyltransferase B; core 4 β6-GalNAc-transferase; core 6β-GalNAc-transferase B; UDP-N-acetyl-D-glucosamine:O-oligosaccharide-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of N-acetyl-β-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-D-galactosaminyl-R 6-β-N-acetyl-D-glucosaminyltransferase
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 95978-15-7
References:
1.  Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356]
[EC 2.4.1.148 created 1984]
 
 
EC 2.4.1.386     Relevance: 61.7%
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 2.4.1.320     Relevance: 61.5%
Accepted name: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase
Reaction: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + α-D-mannose 1-phosphate
Other name(s): BT1033
Systematic name: 4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine:phosphate α-D-mannosyltransferase
Comments: The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nihira, T., Suzuki, E., Kitaoka, M., Nishimoto, M., Ohtsubo, K. and Nakai, H. Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288 (2013) 27366–27374. [DOI] [PMID: 23943617]
[EC 2.4.1.320 created 2014]
 
 
EC 2.4.1.141     Relevance: 61.4%
Accepted name: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + N-acetyl-α-D-glucosaminyl-diphosphodolichol = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase; uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase; N,N′-diacetylchitobiosylpyrophosphoryldolichol synthase; UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-glucosaminyl-diphosphodolichol 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 75536-54-8
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.  Turco, S.J. and Heath, E.C. Glucuronosyl-N-acetylglucosaminyl pyrophosphoryldolichol. Formation in SV40-transformed human lung fibroblasts and biosynthesis in rat lung microsomal preparations. J. Biol. Chem. 252 (1977) 2918–2928. [PMID: 192724]
[EC 2.4.1.141 created 1984]
 
 
EC 2.4.3.10     Relevance: 61.1%
Accepted name: N-acetylglucosaminide α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R
Other name(s): α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc
Systematic name: CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting)
Comments: Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092]
[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10]
 
 
EC 2.4.99.22      
Transferred entry: N-acetylglucosaminide α-(2,6)-sialyltransferase. Now EC 2.4.3.10, N-acetylglucosaminide α-(2,6)-sialyltransferase
[EC 2.4.99.22 created 2020, deleted 2022]
 
 
EC 2.4.1.147     Relevance: 61.1%
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 2.4.1.244     Relevance: 60.9%
Accepted name: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group
Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosamine = N,N′-diacetyllactosediamine
Other name(s): β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Comments: The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534–47544. [DOI] [PMID: 12966086]
2.  Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of β1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134–140. [DOI] [PMID: 15044014]
[EC 2.4.1.244 created 2006]
 
 
EC 2.4.1.280     Relevance: 59.9%
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 2.4.1.201     Relevance: 59.9%
Accepted name: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT4C (gene name); N-acetylglucosaminyltransferase VI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI; uridine diphosphoacetylglucosamine-glycopeptide β-1→4-acetylglucosaminyltransferase VI; mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTVI; GlcNAc-T VI; UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→2)]-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in β1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by β linkages. No homologous enzyme appears to exist in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119699-68-2
References:
1.  Brockhausen, I., Hull, E., Hindsgaul, O., Schachter, H., Shah, R.N., Michnick, S.W. and Carver, J.P. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc β1-6 (GlcNAc β1-2)Man α-R (GlcNAc to Man) β-4-N-acetylglucosaminyltransferase VI. J. Biol. Chem. 264 (1989) 11211–11221. [PMID: 2525556]
2.  Taguchi, T., Ogawa, T., Inoue, S., Inoue, Y., Sakamoto, Y., Korekane, H. and Taniguchi, N. Purification and characterization of UDP-GlcNAc:GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man]-β1,4-N-acetylglucosaminyltransferase VI from hen oviduct. J. Biol. Chem. 275 (2000) 32598–32602. [DOI] [PMID: 10903319]
3.  Sakamoto, Y., Taguchi, T., Honke, K., Korekane, H., Watanabe, H., Tano, Y., Dohmae, N., Takio, K., Horii, A. and Taniguchi, N. Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcβ 1-6(GlcNAcβ 1-2)- manα 1-R[GlcNAc to man]β 1,4N-acetylglucosaminyltransferase VI. J. Biol. Chem. 275 (2000) 36029–36034. [DOI] [PMID: 10962001]
[EC 2.4.1.201 created 1992, modified 2001, modified 2018]
 
 
EC 2.4.1.145     Relevance: 59.7%
Accepted name: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase IV; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV; β-acetylglucosaminyltransferase IV; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase IV; α-1,3-mannosylglycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIV; UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86498-16-0
References:
1.  Gleeson, P.A. and Schachter, H. Control of glycoprotein synthesis. J. Biol. Chem. 258 (1983) 6162–6173. [PMID: 6222042]
2.  Oguri, S., Minowa, M.T., Ihara, Y., Taniguchi, N., Ikenaga, H. and Takeuchi, M. Purification and characterization of UDP-N-acetylglucosamine: α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272 (1997) 22721–22727. [DOI] [PMID: 9278430]
3.  Minowa, M.T., Oguri, S., Yoshida, A., Hara, T., Iwamatsu, A., Ikenaga, H. and Takeuchi, M. cDNA cloning and expression of bovine UDP-N-acetylglucosamine: α1, 3-D-mannoside β1,4-N-acetylglucosaminyltransferase IV. J. Biol. Chem. 273 (1998) 11556–11562. [DOI] [PMID: 9565571]
4.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Oguri, S., Ikenaga, H. and Takeuchi, M. Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine: α1,3-d-mannoside β1, 4-N-acetylglucosaminyltransferase. Glycobiology 9 (1999) 303–310. [DOI] [PMID: 10024668]
5.  Yoshida, A., Minowa, M.T., Takamatsu, S., Hara, T., Ikenaga, H. and Takeuchi, M. A novel second isoenzyme of the human UDP-N-acetylglucosamine:α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconj. J. 15 (1998) 1115–1123. [PMID: 10372966]
6.  Takamatsu, S., Antonopoulos, A., Ohtsubo, K., Ditto, D., Chiba, Y., Le, D.T., Morris, H.R., Haslam, S.M., Dell, A., Marth, J.D. and Taniguchi, N. Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice. Glycobiology 20 (2010) 485–497. [DOI] [PMID: 20015870]
[EC 2.4.1.145 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.227     Relevance: 58%
Accepted name: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
For diagram of peptidoglycan biosynthesis (part 2), click here
Other name(s): MurG transferase; UDP-N-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase (configuration-inverting)
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60976-26-3
References:
1.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 2.4.1.227 created 2002]
 
 
EC 2.4.1.155     Relevance: 57.8%
Accepted name: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT5 (gene name); N-acetylglucosaminyltransferase V; α-mannoside β-1,6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-mannoside β1→6-acetylglucosaminyltransferase; UDP-N-acetylglucosamine:α-mannoside-β1,6 N-acetylglucosaminyltransferase; α-1,3(6)-mannosylglycoprotein β-1,6-N-acetylglucosaminyltransferase; GnTV; GlcNAc-T V; UDP-N-acetyl-D-glucosamine:6-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in β 1-6 linkage to the α-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-90-3
References:
1.  Cummings, R.D., Trowbridge, I.S. and Kornfeld, S. A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257 (1982) 13421–13427. [PMID: 6216250]
2.  Hindsgaul, O., Tahir, S.H., Srivastava, O.P. and Pierce, M. The trisaccharide β-D-GlcpNAc-(1→2)-α-D-Manp-(1→6)-β-D-Manp, as its 8-methoxycarbonyloctyl glycoside, is an acceptor selective for N-acetylglucosaminyltransferase V. Carbohydr. Res. 173 (1988) 263–272. [DOI] [PMID: 2834054]
3.  Shoreibah, M.G., Hindsgaul, O. and Pierce, M. Purification and characterization of rat kidney UDP-N-acetylglucosamine: α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 2920–2927. [PMID: 1531335]
4.  Gu, J., Nishikawa, A., Tsuruoka, N., Ohno, M., Yamaguchi, N., Kangawa, K. and Taniguchi, N. Purification and characterization of UDP-N-acetylglucosamine: α-6-D-mannoside β 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. J. Biochem. 113 (1993) 614–619. [PMID: 8393437]
5.  Park, C., Jin, U.H., Lee, Y.C., Cho, T.J. and Kim, C.H. Characterization of UDP-N-acetylglucosamine:α-6-D-mannoside β-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch. Biochem. Biophys. 367 (1999) 281–288. [PMID: 10395745]
6.  Saito, T., Miyoshi, E., Sasai, K., Nakano, N., Eguchi, H., Honke, K. and Taniguchi, N. A secreted type of β 1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity. J. Biol. Chem. 277 (2002) 17002–17008. [PMID: 11872751]
[EC 2.4.1.155 created 1986, modified 2001, modified 2018]
 
 
EC 2.4.1.197     Relevance: 57.7%
Accepted name: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase
Reaction: Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked α-(1→6) to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum
Other name(s): uridine diphosphoacetylglucosamine-oligosaccharide acetylglucosaminyltransferase; acetylglucosamine-oligosaccharide acetylglucosaminyltransferase; UDP-GlcNAc:oligosaccharide β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide 4-β-N-acetylglucosaminyltransferase
Comments: The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by α-1,3 and α-1,6 links.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123425-54-7
References:
1.  Sharkey, D.J. and Kornfeld, R. Identification of an N-acetylglucosaminyltransferase in Dictyostelium discoideum that transfers an "intersecting" N-acetylglucosamine residue to high mannose oligosaccharides. J. Biol. Chem. 264 (1989) 10411–10419. [PMID: 2525124]
[EC 2.4.1.197 created 1992]
 
 
EC 2.4.1.212     Relevance: 57.1%
Accepted name: hyaluronan synthase
Reaction: (1) UDP-N-acetyl-α-D-glucosamine + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan]
(2) UDP-α-D-glucuronate + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan] = UDP + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan]
For diagram of reaction, click here
Glossary: GlcA = glucuronic acid
Other name(s): spHAS; seHAS; Alternating UDP-α-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase
Systematic name: Alternating UDP-N-acetyl-α-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase (configuration-inverting)
Comments: The enzyme from Streptococcus Group A and Group C requires Mg2+. The enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc [3]. The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in a variety of organisms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39346-43-5
References:
1.  DeAngelis, P.L., Papaconstantinou, J. and Weigel, P.H. Molecular cloning, identification and sequence of the hyaluronan synthase gene from Group A Streptococcus pyogenes. J. Biol. Chem. 268 (1993) 19181–19184. [PMID: 8366070]
2.  Jing, W. and DeAngelis, P.L. Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. Glycobiology 10 (2000) 883–889. [DOI] [PMID: 10988250]
3.  DeAngelis, P.L. Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 274 (1999) 26557–26562. [DOI] [PMID: 10473619]
4.  Tlapak-Simmons, V.L., Baron, C.A. and Weigel, P.H. Characterization of the purified hyaluronan synthase from Streptococcus equisimilis. Biochemistry 43 (2004) 9234–9242. [DOI] [PMID: 15248781]
[EC 2.4.1.212 created 2001, modified 2007]
 
 
EC 2.4.99.1      
Transferred entry: β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022]
 
 
EC 2.4.3.1     Relevance: 56.8%
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]
 
 
EC 2.4.1.355     Relevance: 56%
Accepted name: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase
Reaction: n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-β-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TarS
Systematic name: UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-β-D-glucosamine to the OH group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.70 [poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nathenson, S. G., Strominger, J. L. Enzymatic synthesis of N-acetylglucosaminylribitol linkages in teichoic acid from Staphylococcus aureus, strain Copenhagen. J. Biol. Chem. 238 (1963) 3161–3169. [PMID: 14085356]
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]
3.  Sobhanifar, S., Worrall, L.J., King, D.T., Wasney, G.A., Baumann, L., Gale, R.T., Nosella, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarS, the wall teichoic acid β-glycosyltransferase involved in methicillin resistance. PLoS Pathog. 12:e1006067 (2016). [DOI] [PMID: 27973583]
[EC 2.4.1.355 created 2018]
 
 
EC 2.3.1.3     Relevance: 55.9%
Accepted name: glucosamine N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine
Other name(s): glucosamine acetylase; glucosamine acetyltransferase
Systematic name: acetyl-CoA:D-glucosamine N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-94-4
References:
1.  Chou, T.C. and Soodak, M. The acetylation of D-glucosamine by pigeon liver extracts. J. Biol. Chem. 196 (1952) 105–109. [PMID: 12980946]
[EC 2.3.1.3 created 1961]
 
 
EC 2.4.1.144     Relevance: 55.1%
Accepted name: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-[β-D-GlcNAc-(1→4)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): N-acetylglucosaminyltransferase III; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-glycopeptide β4-acetylglucosaminyltransferase III; β-1,4-mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTIII; GlcNAc-T III; MGAT3 (gene name); UDP-N-acetyl-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. The residue added by the enzyme at position 4 of the β-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc. Unlike GlcNAc residues added to other positions, it is not extended or modified. In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83744-93-8
References:
1.  Narasimhan, S. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide β4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β1-4 linkage to the β-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol. Chem. 257 (1982) 10235–10242. [PMID: 6213618]
2.  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]
3.  Brockhausen, I., Carver, J.P. and Schachter, H. Control of glycoprotein synthesis. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosaminyltransferases I, II, III, IV, V, and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes. Biochem. Cell Biol. 66 (1988) 1134–1151. [PMID: 2975180]
4.  Nishikawa, A., Ihara, Y., Hatakeyama, M., Kangawa, K. and Taniguchi, N. Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: β-D-mannoside β-1,4N-acetylglucosaminyltransferase III from rat kidney. J. Biol. Chem. 267 (1992) 18199–18204. [PMID: 1325461]
5.  Ihara, Y., Nishikawa, A., Tohma, T., Soejima, H., Niikawa, N. and Taniguchi, N. cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J. Biochem. 113 (1993) 692–698. [PMID: 8370666]
[EC 2.4.1.144 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.70     Relevance: 54.6%
Accepted name: poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase
Reaction: n UDP-N-acetyl-α-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-α-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TarM; UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); uridine diphosphoacetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous); UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase (ambiguous); UDP-N-acetyl-α-D-glucosamine:poly(ribitol-phosphate) N-acetyl-α-D-glucosaminyltransferase (ambiguous); poly(ribitol-phosphate) N-acetylglucosaminyltransferase (ambiguous)
Systematic name: UDP-N-acetyl-α-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Comments: Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-α-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.355 [poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-71-7
References:
1.  Nathenson, S.G., Ishimoto, N. and Strominger, J.L. UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases from Staphylococcus aureus. Methods Enzymol. 8 (1966) 426–429.
2.  Xia, G., Maier, L., Sanchez-Carballo, P., Li, M., Otto, M., Holst, O. and Peschel, A. Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM. J. Biol. Chem. 285 (2010) 13405–13415. [DOI] [PMID: 20185825]
3.  Sobhanifar, S., Worrall, L.J., Gruninger, R.J., Wasney, G.A., Blaukopf, M., Baumann, L., Lameignere, E., Solomonson, M., Brown, E.D., Withers, S.G. and Strynadka, N.C. Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase. Proc. Natl. Acad. Sci. USA 112 (2015) E576–E585. [DOI] [PMID: 25624472]
4.  Koc, C., Gerlach, D., Beck, S., Peschel, A., Xia, G. and Stehle, T. Structural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid. J. Biol. Chem. 290 (2015) 9874–9885. [DOI] [PMID: 25697358]
[EC 2.4.1.70 created 1972, modified 2018]
 
 
EC 2.4.1.223     Relevance: 54.6%
Accepted name: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(α-D-GlcNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of heparan biosynthesis (later stages), click here
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): α-N-acetylglucosaminyltransferase I; α1,4-N-acetylglucosaminyltransferase; glucuronosylgalactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl-proteoglycan 4IV-α-N-acetyl-D-glucosaminyltransferase; glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4IV-α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Comments: Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. Apparently products of both the human EXTL2 and EXTL3 genes can catalyse this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. For explanation of the use of a superscript in the systematic name, see 2-Carb-37.2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 179241-74-8
References:
1.  Kitagawa, H., Shimakawa, H. and Sugahara, K. The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274 (1999) 13933–13937. [DOI] [PMID: 10318803]
2.  Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834–4838. [DOI] [PMID: 11121397]
[EC 2.4.1.223 created 2002, modified 2016]
 
 
EC 3.5.1.33     Relevance: 54.2%
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 2.4.1.255     Relevance: 54.1%
Accepted name: protein O-GlcNAc transferase
Reaction: (1) UDP-N-acetyl-α-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine
(2) UDP-N-acetyl-α-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine
Other name(s): O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase
Systematic name: UDP-N-α-acetyl-D-glucosamine:[protein]-3-O-N-acetyl-β-D-glucosaminyl transferase
Comments: Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Banerjee, S., Robbins, P.W. and Samuelson, J. Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum. Glycobiology 19 (2009) 331–336. [DOI] [PMID: 18948359]
2.  Clarke, A.J., Hurtado-Guerrero, R., Pathak, S., Schuttelkopf, A.W., Borodkin, V., Shepherd, S.M., Ibrahim, A.F. and van Aalten, D.M. Structural insights into mechanism and specificity of O-GlcNAc transferase. EMBO J. 27 (2008) 2780–2788. [DOI] [PMID: 18818698]
3.  Rao, F.V., Dorfmueller, H.C., Villa, F., Allwood, M., Eggleston, I.M. and van Aalten, D.M. Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25 (2006) 1569–1578. [DOI] [PMID: 16541109]
4.  Haltiwanger, R.S., Blomberg, M.A. and Hart, G.W. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase. J. Biol. Chem. 267 (1992) 9005–9013. [PMID: 1533623]
5.  Lubas, W.A., Frank, D.W., Krause, M. and Hanover, J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9316–9324. [DOI] [PMID: 9083068]
6.  Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P. and Walker, S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 (2011) 564–567. [DOI] [PMID: 21240259]
[EC 2.4.1.255 created 2011]
 
 
EC 2.7.1.176     Relevance: 54%
Accepted name: UDP-N-acetylglucosamine kinase
Reaction: ATP + UDP-N-acetyl-α-D-glucosamine = ADP + UDP-N-acetyl-α-D-glucosamine 3′-phosphate
Other name(s): UNAG kinase; ζ toxin; toxin PezT; ATP:UDP-N-acetyl-D-glucosamine 3′-phosphotransferase
Systematic name: ATP:UDP-N-acetyl-α-D-glucosamine 3′-phosphotransferase
Comments: Toxic component of a toxin-antitoxin (TA) module. The phosphorylation of UDP-N-acetyl-D-glucosamine results in the inhibition of EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, the first committed step in cell wall synthesis, which is then blocked. The activity of this enzyme is inhibited when the enzyme binds to the cognate ε antitoxin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Khoo, S.K., Loll, B., Chan, W.T., Shoeman, R.L., Ngoo, L., Yeo, C.C. and Meinhart, A. Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae. J. Biol. Chem. 282 (2007) 19606–19618. [DOI] [PMID: 17488720]
2.  Mutschler, H., Gebhardt, M., Shoeman, R.L. and Meinhart, A. A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol. 9:e1001033 (2011). [DOI] [PMID: 21445328]
[EC 2.7.1.176 created 2012]
 
 
EC 5.4.2.3     Relevance: 53.9%
Accepted name: phosphoacetylglucosamine mutase
Reaction: N-acetyl-α-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Other name(s): acetylglucosamine phosphomutase; acetylglucosamine phosphomutase; acetylaminodeoxyglucose phosphomutase; phospho-N-acetylglucosamine mutase; N-acetyl-D-glucosamine 1,6-phosphomutase
Systematic name: N-acetyl-α-D-glucosamine 1,6-phosphomutase
Comments: The enzyme is activated by N-acetyl-α-D-glucosamine 1,6-bisphosphate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-51-4
References:
1.  Carlson, D.M. Phosphoacetylglucosamine mutase from pig submaxillary gland. Methods Enzymol. 8 (1966) 179–182.
2.  Leloir, L.F. and Cardini, C.E. Enzymes acting on glucosamine phosphates. Biochim. Biophys. Acta 20 (1956) 33–42. [PMID: 13315346]
3.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
4.  Reissig, J.L. and Leloir, L.F. Phosphoacetylglucosamine mutase from Neurospora. Methods Enzymol. 8 (1966) 175–178.
[EC 5.4.2.3 created 1961 as EC 2.7.5.2, transferred 1984 to EC 5.4.2.3]
 
 
EC 3.5.1.136     Relevance: 53.4%
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 2.4.1.86     Relevance: 53%
Accepted name: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R
For diagram of lactotetraosylceramide biosynthesis, click here
Other name(s): B3GALT1 (gene name); uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase; glucosaminylgalactosylglucosylceramide β-galactosyltransferase; UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase
Comments: The enzyme transfers galactose from UDP-α-D-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-β-D-glucosamine (β-GlcNAc) residue. It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-46-5
References:
1.  Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489–1495. [PMID: 4335001]
2.  Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270–4274. [DOI] [PMID: 291963]
3.  Amado, M., Almeida, R., Carneiro, F., Levery, S.B., Holmes, E.H., Nomoto, M., Hollingsworth, M.A., Hassan, H., Schwientek, T., Nielsen, P.A., Bennett, E.P. and Clausen, H. A family of human β3-galactosyltransferases. Characterization of four members of a UDP-galactose:β-N-acetyl-glucosamine/β-nacetyl-galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 273 (1998) 12770–12778. [DOI] [PMID: 9582303]
4.  Amado, M., Almeida, R., Schwientek, T. and Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1473 (1999) 35–53. [DOI] [PMID: 10580128]
5.  Bardoni, A., Valli, M. and Trinchera, M. Differential expression of β1,3galactosyltransferases in human colon cells derived from adenocarcinomas or normal mucosa. FEBS Lett. 451 (1999) 75–80. [DOI] [PMID: 10356986]
[EC 2.4.1.86 created 1976, modified 2017]
 
 
EC 2.3.1.4     Relevance: 52.6%
Accepted name: glucosamine-phosphate N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): phosphoglucosamine transacetylase; phosphoglucosamine acetylase; glucosamine-6-phosphate acetylase; D-glucosamine-6-P N-acetyltransferase; aminodeoxyglucosephosphate acetyltransferase; glucosamine 6-phosphate acetylase; glucosamine 6-phosphate N-acetyltransferase; N-acetylglucosamine-6-phosphate synthase; phosphoglucosamine N-acetylase; glucosamine-6-phosphate N-acetyltransferase
Systematic name: acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-91-8
References:
1.  Davidson, E.A. Glucosamine 6-phosphate N-acetylase. Methods Enzymol. 9 (1966) 704–707.
2.  Davidson, E.A., Blumenthal, H.J. and Roseman, F. Glucosamine metabolism. II. Studies of glucosamine 6-phosphate N-acetylase. J. Biol. Chem. 226 (1957) 125–133. [PMID: 13428743]
3.  Pattabiraman, T.N. and Bachhawat, B.K. Purification of glucosamine-6-phosphate N-acetylase from sheep brain. Biochim. Biophys. Acta 59 (1962) 681–689. [DOI] [PMID: 14484387]
4.  Boehmelt, G., Fialka, I., Brothers, G., McGinley, M.D., Patterson, S.D., Mo, R., Hui, C.C., Chung, S., Huber, L.A., Mak, T.W. and Iscove, N.N. Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275 (2000) 12821–12832. [DOI] [PMID: 10777580]
[EC 2.3.1.4 created 1961, modified 2002]
 
 
EC 2.4.1.143     Relevance: 52.2%
Accepted name: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Other name(s): MGAT2 (gene name); N-acetylglucosaminyltransferase II; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mannoside α1→6-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-1,6-mannosylglycoprotein β-1-2-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-α-D-mannoside β1-2-acetylglucosaminyltransferase; UDP-GlcNAc:mannoside α1-6 acetylglucosaminyltransferase; α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTII; GlcNAc-T II; UDP-N-acetyl-D-glucosamine:6-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→6)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its activity initiates the synthesis of the second antenna of di-antennary complex N-glycans. While the natural substrate (produced by EC 3.2.1.114, mannosyl-oligosaccharide 1,3-1,6-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→6)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→3)]-β-D-Man-R.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105913-04-0
References:
1.  Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358]
2.  Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163]
3.  Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827]
4.  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]
5.  Bendiak, B. and Schachter, H. Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:α-D-mannoside β-1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5784–5790. [PMID: 2952645]
6.  Bendiak, B. and Schacter, H. Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:α-D-mannoside β1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem. 262 (1987) 5775–5783. [PMID: 2952644]
7.  Tan, J., D'Agostaro, A.F., Bendiak, B., Reck, F., Sarkar, M., Squire, J.A., Leong, P. and Schachter, H. The human UDP-N-acetylglucosamine: α-6-D-mannoside-β-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein. Eur. J. Biochem. 231 (1995) 317–328. [DOI] [PMID: 7635144]
[EC 2.4.1.143 created 1984, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 2.4.1.101     Relevance: 51.9%
Accepted name: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + Man5GlcNAc2-[protein] = UDP + Man5GlcNAc3-[protein]
For diagram of mannosyl-glycoprotein N-acetylglucosaminyltransferases, click here
Glossary: Man5GlcNAc2-[protein] = α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Man5GlcNAc3-[protein]= β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-N-Asn-[protein]
Other name(s): MGAT1 (gene name); N-acetylglucosaminyltransferase I; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; uridine diphosphoacetylglucosamine-α-1,3-mannosylglycoprotein β-1,2-N-acetylglucosaminyltransferase; UDP-N-acetylglucosaminyl:α-1,3-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I; UDP-N-acetylglucosaminyl:α-3-D-mannoside β-1,2-N-acetylglucosaminyltransferase I; α-1,3-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase; GnTI; GlcNAc-T I; UDP-N-acetyl-D-glucosamine:3-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act. While the natural substrate (produced by EC 3.2.1.113, mannosyl-oligosaccharide 1,2-α-mannosidase) is described here, the minimal substrate recognized by the enzyme is α-D-Man-(1→3)-β-D-Man-R.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102576-81-8
References:
1.  Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity. J. Biol. Chem. 255 (1980) 4885–4893. [PMID: 6445358]
2.  Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa. Biochemistry 20 (1981) 967–976. [PMID: 6452163]
3.  Oppenheimer, C.L. and Hill, R.L. Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799–804. [PMID: 6450208]
4.  Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. The nonidentity of porcine N-acetylglucosaminyltransferases I and II. J. Biol. Chem. 256 (1981) 11477–11482. [PMID: 6457827]
5.  Miyagi, T. and Tsuiki, S. Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas. Biochim. Biophys. Acta 661 (1981) 148–157. [DOI] [PMID: 6170335]
6.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
7.  Vella, G.J., Paulsen, H. and Schachter, H. Control of glycoprotein synthesis. IX. A terminal Man alphal-3Man β1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: α-D-mannoside (GlcNAc to Man α1-3) β2-N-acetylglucosaminyltransferase I. Can. J. Biochem. Cell Biol. 62 (1984) 409–417. [PMID: 6235906]
8.  Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 19 (2000) 5269–5280. [DOI] [PMID: 11032794]
[EC 2.4.1.101 created 1983, modified 2001 (EC 2.4.1.51 created 1972, part incorporated 1984), modified 2018]
 
 
EC 3.5.1.105     Relevance: 51.4%
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 2.4.1.382     Relevance: 51%
Accepted name: CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase
Reaction: CDP-α-D-abequose + 2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = 2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Abe-(1→3)-2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-abequosyl-(1→3)-2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaR (gene name); rfbR (gene name)
Systematic name: CDP-α-D-abequose:2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3IV-α-abequosyltransferase (configuration retaining)
Comments: The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787]
2.  Zhao, X., Dai, Q., Jia, R., Zhu, D., Liu, M., Wang, M., Chen, S., Sun, K., Yang, Q., Wu, Y. and Cheng, A. two novel Salmonella bivalent vaccines confer dual protection against two Salmonella serovars in mice. Front Cell Infect Microbiol 7:391 (2017). [DOI] [PMID: 28929089]
[EC 2.4.1.382 created 2021]
 
 
EC 2.3.1.157     Relevance: 51%
Accepted name: glucosamine-1-phosphate N-acetyltransferase
Reaction: acetyl-CoA + α-D-glucosamine 1-phosphate = CoA + N-acetyl-α-D-glucosamine 1-phosphate
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Systematic name: acetyl-CoA:α-D-glucosamine-1-phosphate N-acetyltransferase
Comments: The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-91-8
References:
1.  Mengin-Lecreulx, D. and van Heijenoort, J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176 (1994) 5788–5795. [DOI] [PMID: 8083170]
2.  Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35 (1996) 579–585. [DOI] [PMID: 8555230]
3.  Olsen, L.R. and Roderick, S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40 (2001) 1913–1921. [DOI] [PMID: 11329257]
[EC 2.3.1.157 created 2001]
 
 
EC 2.4.1.312     Relevance: 50.9%
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 2.4.1.94     Relevance: 50.7%
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 3.2.2.11     Relevance: 50%
Accepted name: β-aspartyl-N-acetylglucosaminidase
Reaction: 1-β-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
Other name(s): β-aspartylacetylglucosaminidase
Systematic name: 1-β-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-31-0
References:
1.  Eylar, E.H. and Murakami, M. β-Aspartyl-N-acetylglucosaminidase from epididymis. Methods Enzymol. 8 (1966) 597–600.
[EC 3.2.2.11 created 1972]
 
 
EC 3.2.1.169     Relevance: 49.3%
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 3.2.1.96     Relevance: 49.3%
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]
 
 


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