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3 mannoside β12 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799-804. [PMID: 6450208]
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 and EC 2.4.1.251 to EC 2.4.1.278
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 2.4.1.278
Accepted name: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 3-(α-D-mannosyl)-β-D-mannosyl-R = UDP + 3-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram click here.
Other name(s): 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
Systematic name: UDP-N-acetyl-D-glucosamine:3-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts before N-acetylglucosaminyltransferases II, III, IV, V and VI (click here for diagram).
Links to other databases: BRENDA, EXPASY, KEGG, 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. 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]
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. Oppenheimer, C.L. and Hill, R.L. Purification and characterization of a rabbit liver α13 mannoside β12 N-acetylglucosaminyltransferase. J. Biol. Chem. 256 (1981) 799-804. [PMID: 6450208]
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 αl-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-D-glucosamine + β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R = UDP + β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(16)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A
Systematic name: 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
Comments: cf. EC 2.4.1.146 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase), EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, 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(GlcNAcGalNAc) 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, 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, 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, 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, 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: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein
Other name(s): dolichol phosphomannose-protein mannosyltransferase; protein O-D-mannosyltransferase
Systematic name: dolichyl-phosphate-D-mannose: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, 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 β-mannosyltransferase
Reaction: GDP-mannose + tRNAAsp-queuosine = GDP + tRNAAsp-O-5"-β-D-mannosylqueuosine
Systematic name: GDP-mannose:tRNAAsp-queuosine O-5"-β-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, 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, 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, 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 1.14.11.19, 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, 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, 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-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
Systematic name: UDP-glucose:dolichyl-phosphate β-D-glucosyltransferase
Comments: Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, 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, 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]
Accepted name: dolichyl-diphosphooligosaccharide—protein glycotransferase
Reaction: dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
Other name(s): dolichyldiphosphooligosaccharide-protein glycosyltransferase; asparagine N-glycosyltransferase; dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase; dolichylpyrophosphodiacetylchitobiose-protein glycosyltransferase; oligomannosyltransferase; oligosaccharide transferase; dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase
Systematic name: dolichyl-diphosphooligosaccharide:protein-L-asparagine oligopolysaccharidotransferase
Comments: Transfers the glucosyl-mannosyl-glucosamine polysaccharide side-chains of glycoproteins to an asparagine residue in the sequence Asn-Xaa-Ser or Asn-Xaa-Thr in the nascent polypeptide chains of the protein moiety.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 75302-32-8
References:
1. Das, R.C. and Heath, E.C. Dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase; solubilization, purification, and properties. Proc. Natl. Acad. Sci. USA 77 (1980) 3811-3815. [PMID: 6933437]
Accepted name: sinapate 1-glucosyltransferase
Reaction: UDP-glucose + sinapate = UDP + 1-sinapoyl-D-glucose
Other name(s): uridine diphosphoglucose-sinapate glucosyltransferase; UDP-glucose:sinapic acid glucosyltransferase; uridine 5'-diphosphoglucose-hydroxycinnamic acid acylglucosyltransferase
Systematic name: UDP-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, 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, 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: glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase
Reaction: UDP-galactose + glycoprotein N-acetyl-D-galactosamine = UDP + glycoprotein D-galactosyl-(1→3)-N-acetyl-D-galactosamine
Other name(s): uridine diphosphogalactose-mucin β-(1→3)-galactosyltransferase
Systematic name: UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase
Comments: The non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: inositol 3-α-galactosyltransferase
Reaction: UDP-galactose + myo-inositol = UDP + O-α-D-galactosyl-(13)-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
Systematic name: UDP-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, 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: sucrose + [(1→6)-α-D-glucosyl]n = D-fructose + [(1→6)-α-D-glucosyl]n+1
Other name(s): water-soluble-glucan synthase; GTF-S; 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
Systematic name: sucrose:(1→6)-α-D-glucan 3(6)-α-D-glucosyltransferase
Comments: Also transfers glucosyl residues to the 3-position on glucose residues in glucans, producing a highly-branched 1,6-α-D-glucan.
Links to other databases: BRENDA, EXPASY, KEGG, 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, 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, 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, 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.
Accepted name: peptidoglycan glycosyltransferase
Reaction: [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
For diagram click here.
Glossary: Mur2Ac = N-acetylmuramic acid
Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
Systematic name: [poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 79079-04-2
References:
1. Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018-5022. [PMID: 6802846]
2. Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079-1093. [PMID: 9841666]
3. van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25R-36R. [PMID: 11320055]
[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-Dol α-1,2-mannosyltransferase
Reaction: 2 GDP-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 GDP + D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol
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
Systematic name: GDP-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 α-1,2-mannosyltransferase
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, 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-Dol α-1,3-mannosyltransferase
Reaction: GDP-D-mannose + D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol
For diagram of reaction click here.
Other name(s): Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 1,3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
Systematic name: GDP-D-mannose:D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase
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, 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-galactose + O-β-D-xylosylprotein = UDP + 4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram click here.
Other name(s): UDP-D-galactose:D-xylose galactosyltransferase; UDP-D-galactose:xylose galactosyltransferase; galactosyltransferase I; uridine diphosphogalactose-xylose galactosyltransferase
Systematic name: UDP-galactose:O-β-D-xylosylprotein 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, 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-galactose + 4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram click here.
Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase
Systematic name: UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 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, 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-glucuronate + 3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein = UDP + 3-β-D-glucuronosyl-3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein
For diagram click here.
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
Systematic name: UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase
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, 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, 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-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:12' galactosyltransferase; floridoside phosphate synthetase; floridoside phosphate synthase
Systematic name: UDP-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, 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-D-glucosamine + (1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-α-D-mannosyl-D-mannose = UDP + (1→3)-α-D-mannosyl-(1→2)-(N-acetyl-α-D-glucosaminyl-α-D-mannosyl)-(1→2)-α-D-mannosyl-D-mannose
Other name(s): α-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine mannoside α12-αcetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:mannotetraose α-N-acetyl-D-glucosaminyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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, 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, 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-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol
For diagram of reaction click here.
Other name(s): UDP-GlcNAc:dolichyl-pyrophosphoryl-GlcNAc GlcNAc transferase; uridine diphosphoacetylglucosamine-dolichylacetylglucosamine pyrophosphate acetylglucosaminyltransferase; N,N'-diacetylchitobiosylpyrophosphoryldolichol synthase
Systematic name: UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol N-acetyl-D-glucosaminyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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-mannose + chitobiosyldiphosphodolichol = GDP + β-(1→4)-D-mannosylchitobiosyldiphosphodolichol
For diagram of reaction click here.
Other name(s): guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase; GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Systematic name: GDP-mannose:chitobiosyldiphosphodolichol β-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, 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-D-glucosamine + 6-(α-D-mannosyl)-β-D-mannosyl-R = UDP + 6-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram click here.
Other name(s): N-acetylglucosaminyltransferase II; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mannoside α16-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
Systematic name: UDP-N-acetyl-D-glucosamine:6-(α-D-mannosyl)-β-D-mannosyl-glycoprotein 2-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor. Note that this enzyme acts after N-acetylglucosaminyltransferase I but before N-acetylglucosaminyltransferases III, IV, V and VI (click here for diagram).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 105913-04-0
References:
1. 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]
2. 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]
3. 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]
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. 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. 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: 2952644]
Accepted name: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-mannosyl-R = UDP + 4-(N-acetyl-β-D-glucosaminyl)-β-D-mannosyl-R
For diagram 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
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor (click here for diagram). The action of this enzyme probably prevents further attachment of N-acetylglucosamine residues to the growing carbohydrate chain.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R = UDP + 3-(2,4-bis[N-acetyl-β-D-glucosaminyl]-α-D-mannosyl)-β-D-mannosyl-R
For diagram 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
Systematic name: UDP-N-acetyl-D-glucosamine:3-[2-(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl]-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Comments: R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor (click here for diagram). The best acceptor for this enzyme is probably the same as that favoured by EC 2.4.1.144, β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→3)-[N-acetyl-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-D-galactosaminyl-R
Other name(s): O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase (elongating); elongation 3β-GalNAc-transferase
Systematic name: UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to -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
Comments: cf. EC 2.4.1.102 (β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase), EC 2.4.1.147 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-β-D-galactosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-β-D-galactosaminyl-R
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
Systematic name: 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
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 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, 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-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-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
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine β-1,3-acetyl-D-glucosaminyltransferase
Comments: Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and other glycoproteins and oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 85638-39-7
References:
1. 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
2. Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β13 and β16 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435-3437. [PMID: 6219989]
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyl-transferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-β-D-glucosaminyl-(1→6)-β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R
Other name(s): N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-GlcNAc:Gal-R, β-D-6-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Comments: Acts on β-galactosyl-(1→4)-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, 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 β13 and β16 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435-3437. [PMID: 6219989]