EC 2.4.1.1 to EC 2.4.1.50See separate file for EC 2.4.1.151 to EC 2.4.1.200, EC 2.4.1.201 to EC 2.4.1.250, EC 2.4.1.251 to EC 2.4.1.300 and EC 2.4.1.301 to EC 2.4.1.397
EC 2.4.1.51 to EC 2.4.1.100
See the following files for:
EC 2.4.1.151 to EC 2.4.1.200
EC 2.4.1.201 to EC 2.4.1.250
EC 2.4.1.251 to EC 2.4.1.300
EC 2.4.1.301 to EC 2.4.1.397
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 reaction 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. [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. [PMID: 11032794]
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. [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]
Accepted name: alizarin 2-β-glucosyltransferase
Reaction: UDP-glucose + 1,2-dihydroxy-9,10-anthraquinone = UDP + 1-hydroxy-2-(β-D-glucosyloxy)-9,10-anthraquinone
Other name(s): uridine diphosphoglucose-alizarin glucosyltransferase
Systematic name: UDP-glucose:1,2-dihydroxy-9,10-anthraquinone 2-O-β-D-glucosyltransferase
Comments: Acts on other hydroxy- and dihydroxy-derivatives of 9,10-anthraquinone.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74506-41-5
References:
1. Mateju, J., Cudlin, J., Steinerova, N., Blumauerova, M. and Vanek, Z. Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens. Folia Microbiol. 24 (1979) 205-210. [PMID: 38193]
Accepted name: o-dihydroxycoumarin 7-O-glucosyltransferase
Reaction: UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin
Other name(s): uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase
Systematic name: UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase
Comments: Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74114-37-7
References:
1. Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177-184.
Accepted name: vitexin β-glucosyltransferase
Reaction: UDP-glucose + vitexin = UDP + vitexin 2"-O-β-D-glucoside
For diagram click here.
Other name(s): uridine diphosphoglucose-vitexin 2"-glucosyltransferase
Systematic name: UDP-glucose:vitexin 2"-O-β-D-glucosyltransferase
Comments: Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76828-68-7
References:
1. Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2"-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935-1937.
Accepted name: isovitexin β-glucosyltransferase
Reaction: UDP-glucose + isovitexin = UDP + isovitexin 2"-O-β-D-glucoside
For diagram click here.
Other name(s): uridine diphosphoglucose-isovitexin 2"-glucosyltransferase
Systematic name: UDP-glucose:isovitexin 2"-O-β-D-glucosyltransferase
Comments: Isovitexin is a flavonoid from petals of Silene alba.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72102-99-9
References:
1. Heinsbroek, R., Van Brederode, J., Van Nigtevecht, G., Maas, J., Kamsteeg, J., Besson, E. and Chopin, J. The 2"-O-glucosylation of vitexin and isovitexin in petals of Silene alba is catalysed by two dfferent enzymes. Phytochemistry 19 (1980) 1935-1937.
[EC 2.4.1.107 Deleted entry: UDP-glucuronate—testosterone glucuronosyltransferase. Now included with EC 2.4.1.17, UDP-glucuronosyltransferase (EC 2.4.1.107 created 1983, deleted 1984)]
[EC 2.4.1.108 Deleted entry: UDP-glucuronate—phenol glucuronosyltransferase. Now included with EC 2.4.1.17, UDP-glucuronosyltransferase (EC 2.4.1.108 created 1983, deleted 1984)]
Accepted name: dolichyl-phosphate-mannose—protein mannosyltransferase
Reaction: (1) dolichyl β-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-threonyl-[protein]
(2) dolichyl β-D-mannosyl phosphate + L-seryl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-seryl-[protein]
For diagram of reaction click here.
Other name(s): dolichol phosphomannose-protein mannosyltransferase; protein O-D-mannosyltransferase; dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase; dolichyl-phosphate-mannose-protein mannosyltransferase
Systematic name: dolichyl-D-mannosyl-phosphate:protein O-D-mannosyltransferase
Comments: The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain α-dihydropolyprenyl derivatives, larger than C35.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74315-99-4
References:
1. Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509-515. [PMID: 6989607]
2. Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517-523. [PMID: 6445267]
Accepted name: tRNA-queuosine α-mannosyltransferase
Reaction: GDP-α-D-mannose + queuosine34 in tRNAAsp = GDP + O-4''-α-D-mannosylqueuosine34 in tRNAAsp
Other name(s): GDP-mannose:tRNAAsp-queuosine O-5''-β-D-mannosyltransferase (incorrect); tRNA-queuosine β-mannosyltransferase (incorrect)
Systematic name: GDP-α-D-mannose:queuosine34 in tRNAAsp O-4''-α-D-mannosyltransferase (configuration-retaining)
Comments: This enzyme, found in higher vertebrates, modifies tRNAAsp at the wobble position of the anticodon loop.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-06-5
References:
1. Okada, N. and Nishimura, S. Enzymatic synthesis of Q nucleoside containing mannose in the anticodon of tRNA: isolation of a novel mannosyltransferase from a cell-free extract of rat liver. Nucleic Acids Res. 4 (1977) 2931-2938. [PMID: 20603]
2. Hillmeier, M., Wagner, M., Ensfelder, T., Korytiakova, E., Thumbs, P., Muller, M. and Carell, T. Synthesis and structure elucidation of the human tRNA nucleoside mannosyl-queuosine. Nat. Commun. 12 (2021) 7123. [PMID: 34880214]
Accepted name: coniferyl-alcohol glucosyltransferase
Reaction: UDP-glucose + coniferyl alcohol = UDP + coniferin
Other name(s): uridine diphosphoglucose-coniferyl alcohol glucosyltransferase; UDP-glucose coniferyl alcohol glucosyltransferase
Systematic name: UDP-glucose:coniferyl-alcohol 4'-β-D-glucosyltransferase
Comments: Sinapyl alcohol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 61116-23-2
References:
1. Ibrahim, R.K. and Grisebach, H. Purification and properties of UDP-glucose: coniferyl alcohol glucosyltransferase from suspension cultures of Paul's scarlet rose. Arch. Biochem. Biophys. 176 (1976) 700-708. [PMID: 10853]
[EC 2.4.1.112 Deleted entry: The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase (EC 2.4.1.112 created 1984, deleted 2007)]
Accepted name: α-1,4-glucan-protein synthase (ADP-forming)
Reaction: ADP-glucose + protein = ADP + α-D-glucosyl-protein
Other name(s): ADP-glucose:protein glucosyltransferase; adenosine diphosphoglucose-protein glucosyltransferase
Systematic name: ADP-glucose:protein 4-α-D-glucosyltransferase
Comments: The enzyme builds up α-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 67053-99-0
References:
1. Barengo, R. and Krisman, C.R. Initiation of glycogen biosynthesis in Escherichia coli. Studies of the properties of the enzymes involved. Biochim. Biophys. Acta 540 (1978) 190-196. [PMID: 418819]
Accepted name: 2-coumarate O-β-glucosyltransferase
Reaction: UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-β-D-glucosyl-2-hydroxycinnamate
Other name(s): uridine diphosphoglucose-o-coumarate glucosyltransferase; UDPG:o-coumaric acid O-glucosyltransferase
Systematic name: UDP-glucose:trans-2-hydroxycinnamate O-β-D-glucosyltransferase
Comments: Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73665-97-1
References:
1. Kleinhofs, A., Haskins, F.A. and Gorz, H.J. trans-o-Hydroxylcinnamic acid glucosylation in cell-free extracts of Melilotus alba. Phytochemistry 6 (1967) 1313-1318.
2. Poulton, J.E., McRee, B.E. and Conn, E.E. Intracellular localization of two enzymes involved in coumarin biosynthesis in Melilotus alba. Plant Physiol. 65 (1980) 171-175.
Accepted name: anthocyanidin 3-O-glucosyltransferase
Reaction: UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside
For diagram click here.
Other name(s): uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT
Systematic name: UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase
Comments: The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.20.4, leucocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65607-32-1
References:
1. Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045-1058. [PMID: 751640]
2. Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224-9233. [PMID: 9535914]
3. Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797-25803. [PMID: 11316805]
Accepted name: cyanidin 3-O-rutinoside 5-O-glucosyltransferase
Reaction: UDP-glucose + cyanidin 3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside
For diagram click here.
Glossary: cyanidin 3-O-rutinoside = cyanidin-3-O-β-L-rhamnosyl-(1→6)-β-D-glucoside
Other name(s): uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase
Systematic name: UDP-glucose:cyanidin-3-O-β-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase
Comments: Also acts on pelargonidin-3-rutinoside. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin-3-glucoside.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70248-66-7
References:
1. Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059-1071. [PMID: 751641]
Accepted name: dolichyl-phosphate β-glucosyltransferase
Reaction: UDP-α-D-glucose + dolichyl phosphate = UDP + dolichyl β-D-glucosyl phosphate
Other name(s): polyprenyl phosphate:UDP-D-glucose glucosyltransferase; UDP-glucose dolichyl-phosphate glucosyltransferase; uridine diphosphoglucose-dolichol glucosyltransferase; UDP-glucose:dolichol phosphate glucosyltransferase; UDP-glucose:dolicholphosphoryl glucosyltransferase; UDP-glucose:dolichyl monophosphate glucosyltransferase; UDP-glucose:dolichyl phosphate glucosyltransferase; UDP--glucose:dolichyl-phosphate β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:dolichyl-phosphate β-D-glucosyltransferase (configuration-inverting)
Comments: Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 71061-42-2
References:
1. Behrens, N.H. and Leloir, L.F. Dolichol monophosphate glucose: an intermediate in glucose transfer in liver. Proc. Natl. Acad. Sci. USA 66 (1970) 153-159. [PMID: 5273893]
2. Herscovics, A., Bugge, B. and Jeanloz, R.W. Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. J. Biol. Chem. 252 (1977) 2271-2277. [PMID: 849929]
3. Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate: UDP-D-glucose glucosyltransferase. J. Biol. Chem. 254 (1979) 4814-4819. [PMID: 438216]
Reaction: UDP-glucose + an N6-alkylaminopurine = UDP + an N6-alkylaminopurine-7-β-D-glucoside
Glossary:
zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
Other name(s): uridine diphosphoglucose-zeatin 7-glucosyltransferase; cytokinin 7-glucosyltransferase; UDP-glucose:zeatin 7-glucosyltransferase
Systematic name: UDP-glucose:N6-alkylaminopurine 7-glucosyltransferase
Comments: Acts on a range of N6-substituted adenines, including zeatin and N6-benzylaminopurine, but not N6-benzyladenine. With some acceptors, 9-β-D-glucosides are also formed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72103-03-8
References:
1. Entsch, B. and Letham, D.S. Enzymic glucosylation of the cytokinin, 6-benzylaminopurine. Plant Sci. Lett. 14 (1979) 205-212.
2. Entsch, B., Parker, C.W., Letham, D.S. and Summons, R.E. Preparation and characterization, using high-performance liquid chromatography, of an enzyme forming glucosides of cytokinins. Biochim. Biophys. Acta 570 (1979) 124-139. [PMID: 486500]
[EC 2.4.1.119 Transferred entry: dolichyl-diphosphooligosaccharideprotein glycotransferase. As the enzyme transfers more than one hexosyl group, it has been transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase (EC 2.4.1.119 created 1984, deleted 2012)]
Accepted name: sinapate 1-glucosyltransferase
Reaction: UDP-α-D-glucose + sinapate = UDP + 1-O-sinapoyl-β-D-glucose
Glossary: sinapate = (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate
Other name(s): uridine diphosphoglucose-sinapate glucosyltransferase; UDP-glucose:sinapic acid glucosyltransferase; uridine 5′-diphosphoglucose-hydroxycinnamic acid acylglucosyltransferase; UDP-glucose:sinapate D-glucosyltransferase
Systematic name: UDP-α-D-glucose:sinapate D-glucosyltransferase
Comments: Some other hydroxycinnamates, including 4-coumarate, ferulate and caffeate, can act as acceptors, but more slowly. Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126 hydroxycinnamate 4-β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 74082-53-4
References:
1. Strack, D. Enzymatic synthesis of 1-sinapoylglucose from free sinapic acid and UDP-glucose by a cell free system from Raphanus sativus seedlings. Z. Naturforsch. C: Biosci. 35 (1980) 204-208.
Accepted name: indole-3-acetate β-glucosyltransferase
Reaction: UDP-glucose + (indol-3-yl)acetate = UDP + 1-O-(indol-3-yl)acetyl-β-D-glucose
Other name(s): uridine diphosphoglucose-indoleacetate glucosyltransferase; UDPG-indol-3-ylacetyl glucosyl transferase; UDP-glucose:indol-3-ylacetate glucosyltransferase; indol-3-ylacetylglucose synthase; UDP-glucose:indol-3-ylacetate glucosyl-transferase; IAGlu synthase; IAA-glucose synthase; UDP-glucose:indole-3-acetate β-D-glucosyltransferase
Systematic name: UDP-glucose:(indol-3-yl)acetate β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74082-56-7
References:
1. Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273-281. [PMID: 6218801]
Accepted name: N-acetylgalactosaminide β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-R
Other name(s): glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase; uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase; UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase; UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase; wbnJ (gene name); wbiP (gene name); C1GALT1 (gene name); UDP-α-D-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-galactosaminyl-R β-1,3-galactosyltransferase (configuration-inverting)
Comments: The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-61-7
References:
1. Hesford, F.J., Berger, E.G. and van den Eijnden, D.H. Identification of the product formed by human erythrocyte galactosyltransferase. Biochim. Biophys. Acta 659 (1981) 302-311. [PMID: 6789880]
2. Mendicino, J., Sivakami, S., Davila, M. and Chandrasekaran, E.V. Purification and properties of UDP-gal:N-acetylgalactosaminide mucin:β1,3-galactosyltransferase from swine trachea mucosa. J. Biol. Chem. 257 (1982) 3987-3994. [PMID: 6801057]
3. 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]
4. Ju, T., Brewer, K., D'Souza, A., Cummings, R.D. and Canfield, W.M. Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277 (2002) 178-186. [PMID: 11677243]
5. Yi, W., Perali, R.S., Eguchi, H., Motari, E., Woodward, R. and Wang, P.G. Characterization of a bacterial β-1,3-galactosyltransferase with application in the synthesis of tumor-associated T-antigen mimics. Biochemistry 47 (2008) 1241-1248. [PMID: 18179256]
6. Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418-423. [PMID: 20418877]
Accepted name: inositol 3-α-galactosyltransferase
Reaction: UDP-α-D-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol
For diagram of reaction click here.
Glossary: galactinol = 3-O-α-D-galactosyl-1D-myo-inositol
Other name(s): UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase; GolS; UDP-galactose:myo-inositol 3-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:myo-inositol 3-α-D-galactosyltransferase
Comments: An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 79955-89-8
References:
1. Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25-33.
[EC 2.4.1.124 Transferred entry: now included with EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase (EC 2.4.1.124 created 1984, deleted 2002)]
Accepted name: sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase
Reaction: (1) sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + [(1→6)-α-D-glucosyl]n+1
(2) sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + (1→3)-α-D-glucosyl[(1→6)-α-D-glucosyl]n
Other name(s): water-soluble-glucan synthase; GTF-S; GTF-S; GTF-SI; sucrose-1,6-α-glucan 3(6)-α-glucosyltransferase; sucrose:1,6-α-D-glucan 3-α- and 6-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase; gtfB (gene name); gtfC (gene name); gtfD (gene name)
Systematic name: sucrose:(1→6)-α-D-glucan 3(6)-α-D-glucosyltransferase
Comments: The enzyme was characterized from the dental caries bacterium Streptococcus mutans. It transfers glucosyl residues from sucrose to either the 6- or the 3-positions of glucose residues in glucans, producing a highly-branched extracellular D-glucan polymers that promote attachment of the bacteria to teeth. Three types of the enzyme have been described; the insoluble polymers produced by GTF-I and GTF-SI contain 85% α(1→3) bonds and 15% α(1→6) bonds, while the soluble polymers produced by GTF-S contain only 30% of α(1→3) bonds and 70% α(1→6) bonds. cf. EC 2.4.1.5, dextransucrase [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81725-87-3
References:
1. Mukasa, H., Shimamura, A. and Tsumori, H. Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c. Biochim. Biophys. Acta 719 (1982) 81-89. [PMID: 6216919]
2. Shimamura, A., Tsumori, H. and Mukasa, H. Purification and properties of Streptococcus mutans extracellular glucosyltransferase. Biochim. Biophys. Acta 702 (1982) 72-80. [PMID: 6461359]
3. Tsumori, H., Shimamura, A. and Mukasa, H. Purification and properties of extracellular glucosyltransferase synthesizing 1,6-, 1,3-α-D-glucan from Streptococcus mutans serotype a. J. Gen. Microbiol. 131 (1985) 3347-3353. [PMID: 2937877]
Accepted name: hydroxycinnamate 4-β-glucosyltransferase
Reaction: UDP-glucose + trans-4-hydroxycinnamate = UDP + 4-O-β-D-glucosyl-4-hydroxycinnamate
Other name(s): uridine diphosphoglucose-hydroxycinnamate glucosyltransferase; UDP-glucose-hydroxycinnamate glucosyltransferase; hydroxycinnamoyl glucosyltransferase
Systematic name: UDP-glucose:trans-4-hydroxycinnamate 4-O-β-D-glucosyltransferase
Comments: Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120 sinapate 1-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 77848-85-2
References:
1. Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967-972.
Accepted name: monoterpenol β-glucosyltransferase
Reaction: UDP-glucose + (–)-menthol = UDP + (–)-menthyl O-β-D-glucoside
For diagram click here.
Other name(s): uridine diphosphoglucose-monoterpenol glucosyltransferase; UDPglucose:monoterpenol glucosyltransferase
Systematic name: UDP-glucose:(–)-menthol O-β-D-glucosyltransferase
Comments: (+)-Neomenthol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78990-64-4
References:
1. Fleuriet, A., Macheix, J.J., Suen, R. and Ibrahim, R.K. Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from tomato fruits. Z. Naturforsch. C: Biosci. 35 (1980) 967-972.
Accepted name: scopoletin glucosyltransferase
Reaction: UDP-glucose + scopoletin = UDP + scopolin
Other name(s): uridine diphosphoglucose-scopoletin glucosyltransferase; UDP-glucose:scopoletin glucosyltransferase; SGTase
Systematic name: UDP-glucose:scopoletin O-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81210-69-7
References:
1. Hino, F., Okazaki, M. and Miura, Y. Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of scopoletin to scopolin in tobacco tissue-culture. Plant Physiol. 69 (1982) 810-813.
[EC 2.4.1.129 Transferred entry: peptidoglycan glycosyltransferase. Now EC 2.4.99.28, peptidoglycan glycosyltransferase (EC 2.4.1.129 created 1984, modified 2002, deleted 2023)]
[EC 2.4.1.130 Transferred entry: dolichyl-phosphate-mannose—glycolipid α-mannosyltransferase. Now covered by EC 2.4.1.258 (Dol-P-Man:Man5GlcNAc2-PP-Dol α-1,3-mannosyltransferase), EC 2.4.1.259 (Dol-P-Man:Man6GlcNAc2-PP-Dol α-1,2-mannosyltransferase), EC 2.4.1.260 (Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase) and EC 2.4.1.261 (Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase). (EC 2.4.1.130 created 1984, deleted 2011)]
Accepted name: GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: 2 GDP-α-D-mannose + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of reaction click here.
Other name(s): ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man3GlcNAc2-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase
Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1→2) linkages to the nascent oligosaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 74506-43-7
References:
1. O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593-9603. [PMID: 16878994]
2. Absmanner, B., Schmeiser, V., Kampf, M. and Lehle, L. Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an α1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. Biochem. J. 426 (2010) 205-217. [PMID: 19929855]
3. Schutzbach, J.S., Springfield, J.D. and Jensen, J.W. The biosynthesis of oligosaccharide-lipids. Formation of an α-1,2-mannosyl-mannose linkage. J. Biol. Chem. 255 (1980) 4170-4175. [PMID: 6154707]
Accepted name: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
Reaction: GDP-α-D-mannose + β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of reaction click here
Glossary: β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = β-D-mannosyl-(1→4)-N,N′-diacetylchitobiosyldiphosphodolichol
Other name(s): Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase
Systematic name: GDP-α-D-mannose:β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81181-76-2
References:
1. Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900-11912. [PMID: 19282279]
2. O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593-9603. [PMID: 16878994]
Accepted name: xylosylprotein 4-β-galactosyltransferase
Reaction: UDP-α-D-galactose + O-β-D-xylosyl-[protein] = UDP + 4-β-D-galactosyl-O-β-D-xylosyl-[protein]
For diagram click here.
Other name(s): UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase; UDP-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase; UDP-α-D-galactose:O-β-D-xylosylprotein 4-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:O-β-D-xylosyl-[protein] 4-β-D-galactosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52227-72-2
References:
1. Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200-5207. [PMID: 1150655]
2. Okajima, T., Yoshida, K., Kondo, T. and Furukawa, K. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 274 (1999) 22915-22918. [PMID: 10438455]
Accepted name: galactosylxylosylprotein 3-β-galactosyltransferase
Reaction: UDP-α-D-galactose + 4-β-D-galactosyl-O-β-D-xylosyl-[protein] = UDP + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-[protein]
For diagram click here.
Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase; UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase; UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosyl-[protein] 3-β-D-galactosyltransferase
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56626-21-2 and 56626-19-8
References:
1. Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805-814. [PMID: 3924029]
2. Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200-5207. [PMID: 1150655]
3. Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189-48195. [PMID: 11551958]
Accepted name: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of reaction click here.
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:[protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine D-glucuronosyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 227184-75-0
References:
1. Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799-2805. [PMID: 5770003]
2. Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327-4332. [PMID: 4260846]
3. Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615-6618. [PMID: 9506957]
Accepted name: gallate 1-β-glucosyltransferase
Reaction: UDP-glucose + gallate = UDP + 1-galloyl-β-D-glucose
Other name(s): UDP-glucose—vanillate 1-glucosyltransferase; UDPglucose:vanillate 1-O-glucosyltransferase; UDPglucose:gallate glucosyltransferase
Systematic name: UDP-glucose:gallate β-D-glucosyltransferase
Comments: A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors. Vanillin is the best acceptor investigated.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 89700-30-1
References:
1. Gross, G.G. Synthesis of β-glucogallin from UDP-glucose and gallic acid by an enzyme preparation from oak leaves. FEBS Lett. 148 (1982) 67-70.
2. Gross, G.G. Partial-purification and properties of UDP-glucose-vanillate 1-O-glucosyl transferase from oak leaves. Phytochemistry 22 (1983) 2179-2182.
Accepted name: sn-glycerol-3-phosphate 2-α-galactosyltransferase
Reaction: UDP-α-D-galactose + sn-glycerol 3-phosphate = UDP + 2-(α-D-galactosyl)-sn-glycerol 3-phosphate
Other name(s): floridoside-phosphate synthase; UDP-galactose:sn-glycerol-3-phosphate-2-D-galactosyl transferase; FPS; UDP-galactose, sn-3-glycerol phosphate:1→2' galactosyltransferase; floridoside phosphate synthetase; floridoside phosphate synthase; UDP-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:sn-glycerol-3-phosphate 2-α-D-galactosyltransferase
Comments: The product is hydrolysed by a phosphatase to floridoside (cf. EC 2.4.1.96 sn-glycerol-3-phosphate 1-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 80747-34-8
References:
1. Gray, N.C.C. and Strickland, K.P. The purification and characterization of a phospholipase A2 activity from the 106,000 x g pellet (microsomal fraction) of bovine brain acting on phosphatidylinositol. Can. J. Biochem. 60 (1982) 108-117. [PMID: 7083039]
Accepted name: mannotetraose 2-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man = UDP + α-D-Man-(1→3)-[α-D-GlcNAc-(1→2)]-α-D-Man-(1→2)-α-D-Man-(1→2)-D-Man
Other name(s): α-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine mannoside α1→2-αcetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:mannotetraose α-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-D-mannose α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81032-47-5
References:
1. Douglas, R.H. and Ballou, C.E. Purification of an α-N-acetylglucosaminyltransferase from the yeast Kluyveromyces lactis and a study of mutants defective in this enzyme activity. Biochemistry 21 (1982) 1561-1570. [PMID: 6211189]
Accepted name: maltose synthase
Reaction: 2 α-D-glucose 1-phosphate + H2O = maltose + 2 phosphate
Systematic name: α-D-glucose-1-phosphate:α-D-glucose-1-phosphate 4-α-D-glucosyltransferase (dephosphorylating)
Comments: Neither free phosphate nor maltose 1-phosphate is an intermediate in the reaction.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81669-74-1
References:
1. Schilling, N. Characterization of maltose biosynthesis from α-D-glucose-1-phosphate in Spinacia oleracea L. Planta 154 (1982) 87-93.
Accepted name: alternansucrase
Reaction: Transfers alternately an α-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an α-D-glucan, thus producing a glucan having alternating (1→6)-α- and (1→3)-α-linkages
Other name(s): sucrose-1,6(3)-α-glucan 6(3)-α-glucosyltransferase; sucrose:1,6-, 1,3-α-D-glucan 3-α- and 6-α-D-glucosyltransferase
Systematic name: sucrose:1,6(1,3)-α-D-glucan 6(3)-α-D-glucosyltransferase
Comments: The product, which has quite different properties from other dextrans, has been called alternan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 100630-46-4
References:
1. Cote, G.L. and Robyt, J.F. Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1→6), (1→3)-α-D-glucan. Carbohydr. Res. 101 (1982) 57-74. [PMID: 7060056]
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 reaction 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. [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]
Accepted name: chitobiosyldiphosphodolichol β-mannosyltransferase
Reaction: GDP-α-D-mannose + N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = GDP + β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of reaction click here.
Glossary: N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol = N,N′-diacetylchitobiosyl-diphosphodolichol
Other name(s): guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose:chitobiosyldiphosphodolichol β-D-mannosyltransferase
Systematic name: GDP-α-D-mannose:N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphosphodolichol 4-β-D-mannosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83380-85-2
References:
1. Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319-325. [PMID: 6215245]
2. Takahashi, T., Honda, R. and Nishikawa, Y. Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology 10 (2000) 321-327. [PMID: 10704531]
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 reaction 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. [PMID: 7635144]
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 reaction 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]
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 reaction 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. [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. [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. [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. [PMID: 20015870]
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. [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]
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. [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. [PMID: 7655172]
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
Systematic name: 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
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. [PMID: 6226356]
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 β1-3- and β1-6-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]
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 β 1-3Gal(-R) β 1-6(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. [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. [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. [PMID: 9915862]