The Enzyme Database

Displaying entries 151-200 of 393.

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EC 2.4.1.184     
Accepted name: galactolipid galactosyltransferase
Reaction: 2 a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[β-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Glossary: a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = monogalactosyldiacylglycerol
Other name(s): galactolipid-galactolipid galactosyltransferase; galactolipid:galactolipid galactosyltransferase; interlipid galactosyltransferase; GGGT; DGDG synthase (ambiguous); digalactosyldiacylglycerol synthase (ambiguous); 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; SFR2 (gene name)
Systematic name: 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol β-D-galactosyltransferase
Comments: The enzyme converts monogalactosyldiacylglycerol to digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol. All residues are connected by β linkages. The activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants, which is performed by EC 2.4.1.46, monogalactosyldiacylglycerol synthase, and EC 2.4.1.241, digalactosyldiacylglycerol synthase. Note that the β,β-digalactosyldiacylglycerol formed by this enzyme is different from the more common α,β-digalactosyldiacylglycerol formed by EC 2.4.1.241. The enzyme provides an important mechanism for the stabilization of the chloroplast membranes during freezing and drought stress.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66676-74-2
References:
1.  Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R. The galactolipid-galactolipid galactosyltransferase is located on the outer surface of the outer-membrane of the chloroplast envelope. FEBS Lett. 145 (1982) 30–34.
2.  Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envelope membrane of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281–289.
3.  Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M. UDPgalactose-independent synthesis of monogalactosyldiacylglycerol. An enzymatic activity of the spinach chloroplast envelope. Biochim. Biophys. Acta 961 (1988) 38–47. [DOI]
4.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
5.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
6.  Fourrier, N., Bedard, J., Lopez-Juez, E., Barbrook, A., Bowyer, J., Jarvis, P., Warren, G. and Thorlby, G. A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against freeze-induced damage in Arabidopsis. Plant J. 55 (2008) 734–745. [DOI] [PMID: 18466306]
7.  Moellering, E.R., Muthan, B. and Benning, C. Freezing tolerance in plants requires lipid remodeling at the outer chloroplast membrane. Science 330 (2010) 226–228. [DOI] [PMID: 20798281]
[EC 2.4.1.184 created 1990, modified 2005, modified 2015]
 
 
EC 2.4.1.185     
Accepted name: flavanone 7-O-β-glucosyltransferase
Reaction: UDP-glucose + a flavanone = UDP + a flavanone 7-O-β-D-glucoside
For diagram of the biosynthesis of naringenin derivatives, click here
Other name(s): uridine diphosphoglucose-flavanone 7-O-glucosyltransferase; naringenin 7-O-glucosyltransferase; hesperetin 7-O-glucosyl-transferase
Systematic name: UDP-glucose:flavanone 7-O-β-D-glucosyltransferase
Comments: Naringenin and hesperetin can act as acceptors. No action on flavones or flavonols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-73-0
References:
1.  McIntosh, C.A., Latchinian, L. and Mansell, R.L. Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: purification and characterization. Arch. Biochem. Biophys. 282 (1990) 50–57. [DOI] [PMID: 2171434]
2.  McIntosh, C.A. and Mansell, R.L. Biosynthesis of naringin in Citrus paradisi - UDP-glucosyl-transferase activity in grapefruit seedlings. Phytochemistry 29 (1990) 1533–1538.
[EC 2.4.1.185 created 1992]
 
 
EC 2.4.1.186     
Accepted name: glycogenin glucosyltransferase
Reaction: UDP-α-D-glucose + glycogenin = UDP + α-D-glucosylglycogenin
Other name(s): glycogenin; priming glucosyltransferase; UDP-glucose:glycogenin glucosyltransferase
Systematic name: UDP-α-D-glucose:glycogenin α-D-glucosyltransferase
Comments: The first reaction of this enzyme is to catalyse its own glucosylation, normally at Tyr-194 of the protein if this group is free. When Tyr-194 is replaced by Thr or Phe, the enzyme’s Mn2+-dependent self-glucosylation activity is lost but its intermolecular transglucosylation ability remains [7]. It continues to glucosylate an existing glucosyl group until a length of about 5–13 residues has been formed. Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11, glycogen (starch) synthase. The enzyme is not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. Similarly it is not highly specific for the acceptor, using water (i.e. hydrolysing UDP-glucose) among others. Various forms of the enzyme exist, and different forms predominate in different organs. Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117590-73-5
References:
1.  Krisman, C.R. and Barengo, R. A precursor of glycogen biosynthesis: α-1,4-glucan-protein. Eur. J. Biochem. 52 (1975) 117–123. [DOI] [PMID: 809265]
2.  Pitcher, J., Smythe, C., Campbell, D.G. and Cohen, P. Identification of the 38-kDa subunit of rabbit skeletal muscle glycogen synthase as glycogenin. Eur. J. Biochem. 169 (1987) 497–502. [DOI] [PMID: 3121316]
3.  Pitcher, J., Smythe, C. and Cohen, P. Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176 (1988) 391–395. [DOI] [PMID: 2970965]
4.  Kennedy, L.D., Kirkman, B.R., Lomako, J., Rodriguez, I.R. and Whelan, W.J. The biogenesis of rabbit-muscle glycogen. In: Berman, M.C. and Opie, L.A. (Ed.), Membranes and Muscle, ICSU Press/IRL Press, Oxford, 1985, pp. 65–84.
5.  Rodriguez, I.R. and Whelan, W.J. A novel glycosyl-amino acid linkage: rabbit-muscle glycogen is covalently linked to a protein via tyrosine. Biochem. Biophys. Res. Commun. 132 (1985) 829–836. [DOI] [PMID: 4062948]
6.  Lomako, J., Lomako, W.M. and Whelan, W.J. A self-glucosylating protein is the primer for rabbit muscle glycogen biosynthesis. FASEB J. 2 (1988) 3097–3103. [PMID: 2973423]
7.  Alonso, M.D., Lomako, J., Lomako, W.M. and Whelan, W.J. Catalytic activities of glycogenin additional to autocatalytic self-glucosylation. J. Biol. Chem. 270 (1995) 15315–15319. [DOI] [PMID: 7797519]
8.  Alonso, M.D., Lomako, J., Lomako, W.M. and Whelan, W.J. A new look at the biogenesis of glycogen. FASEB J. 9 (1995) 1126–1137. [PMID: 7672505]
9.  Mu, J. and Roach, P.J. Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism. J. Biol. Chem. 273 (1998) 34850–34856. [DOI] [PMID: 9857012]
10.  Gibbons, B.J., Roach, P.J. and Hurley, T.D. Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin. J. Mol. Biol. 319 (2002) 463. [DOI] [PMID: 12051921]
[EC 2.4.1.186 created 1992 (EC 2.4.1.112 created 1984, incorporated 2007)]
 
 
EC 2.4.1.187     
Accepted name: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase
Reaction: UDP-N-acetyl-α-D-mannosamine + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): uridine diphosphoacetyl-mannosamineacetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminyltransferase; N-acetylmannosaminyltransferase; UDP-N-acetylmannosamine:N-acetylglucosaminyl diphosphorylundecaprenol N-acetylmannosaminyltransferase; UDP-N-acetyl-D-mannosamine:N-acetyl-β-D-glucosaminyldiphosphoundecaprenol β-1,4-N-acetylmannosaminyltransferase; UDP-N-acetyl-D-mannosamine:N-acetyl-β-D-glucosaminyldiphosphoundecaprenol 4-β-N-acetylmannosaminyltransferase; tagA (gene name); tarA (gene name); UDP-N-acetyl-α-D-mannosamine:N-acetyl-β-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-β-N-acetylmannosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-mannosamine:N-acetyl-α-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol 4-β-N-acetylmannosaminyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 118731-82-1
References:
1.  Murazumi, N., Kumita, K., Araki, Y. and Ito, E. Partial purification and properties of UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase from Bacillus subtilis. J. Biochem. (Tokyo) 104 (1988) 980–984. [PMID: 2977387]
2.  Ginsberg, C., Zhang, Y.H., Yuan, Y. and Walker, S. In vitro reconstitution of two essential steps in wall teichoic acid biosynthesis. ACS Chem. Biol. 1 (2006) 25–28. [DOI] [PMID: 17163636]
3.  Zhang, Y.H., Ginsberg, C., Yuan, Y. and Walker, S. Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA. Biochemistry 45 (2006) 10895–10904. [DOI] [PMID: 16953575]
[EC 2.4.1.187 created 1992, modified 2016]
 
 
EC 2.4.1.188     
Accepted name: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase
Reaction: UDP-α-D-glucose + N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-glucosyl-(1→4)-N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase; uridine diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol glucosyltransferase; UDP-glucose:N-acetyl-D-glucosaminyldiphosphoundecaprenol 4-β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acetyl-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118731-83-2
References:
1.  Kumita, K., Murazumi, N., Arasaki, Y. and Ito, E. Solubilization and properties of UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase from Bacillus coagulans AHU 1366 membranes. J. Biochem. (Tokyo) 104 (1988) 985–988. [PMID: 2977388]
[EC 2.4.1.188 created 1992]
 
 
EC 2.4.1.189     
Accepted name: luteolin 7-O-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + luteolin = UDP + luteolin 7-O-β-D-glucuronide
For diagram of luteolin derivatives biosynthesis, click here
Other name(s): uridine diphosphoglucuronate-luteolin 7-O-glucuronosyltransferase; LGT; UDP-glucuronate:luteolin 7-O-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:luteolin 7-O-glucuronosyltransferase (configuration-inverting)
Comments: The enzyme participates in the biosynthesis of luteolin triglucuronide, the major flavone found in the photosynthetically-active mesophyll of the primary leaves of Secale cereale (rye).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115490-49-8
References:
1.  Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261–1267.
[EC 2.4.1.189 created 1992]
 
 
EC 2.4.1.190     
Accepted name: luteolin-7-O-glucuronide 2′′-O-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + luteolin 7-O-β-D-glucuronide = UDP + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide]
For diagram of luteolin derivatives biosynthesis, click here
Other name(s): uridine diphosphoglucuronate-luteolin 7-O-glucuronide glucuronosyltransferase; LMT; UDP-glucuronate:luteolin 7-O-glucuronide-glucuronosyltransferase; UDP-glucuronate:luteolin-7-O-β-D-glucuronide 2′′-O-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:luteolin-7-O-β-D-glucuronide 2′′-O-glucuronosyltransferase (configuration-inverting)
Comments: The enzyme participates in the biosynthesis of luteolin triglucuronide, the major flavone found in the photosynthetically-active mesophyll of the primary leaves of Secale cereale (rye).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115490-51-2
References:
1.  Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261–1267.
2.  Anhalt, S. and Weissenböck, G. Subcellular localization of luteolin glucuronides and related enzymes in rye mesophyll. Planta 187 (1992) 83–88. [PMID: 24177970]
[EC 2.4.1.190 created 1992]
 
 
EC 2.4.1.191     
Accepted name: luteolin-7-O-diglucuronide 4′-O-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide] = UDP + luteolin 7-O-[β-D-glucuronosyl-(1→2)-β-D-glucuronide]-4′-O-β-D-glucuronide
For diagram of luteolin derivatives biosynthesis, click here
Other name(s): uridine diphosphoglucuronate-luteolin 7-O-diglucuronide glucuronosyltransferase; UDP-glucuronate:luteolin 7-O-diglucuronide-glucuronosyltransferase; UDPglucuronate:luteolin 7-O-diglucuronide-4′-O-glucuronosyl-transferase; LDT; UDP-glucuronate:luteolin-7-O-β-D-diglucuronide 4′-O-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:luteolin-7-O-β-D-diglucuronide 4′-O-glucuronosyltransferase (configuration-inverting)
Comments: The enzyme participates in the biosynthesis of luteolin triglucuronide, the major flavone found in the photosynthetically-active mesophyll of the primary leaves of Secale cereale (rye).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115490-50-1
References:
1.  Schulz, M. and Weissenböck, G. 3 specific UDP-glucuronate-flavone-glucuronosyl-transferases from primary leaves of Secale cereale. Phytochemistry 27 (1988) 1261–1267.
[EC 2.4.1.191 created 1992, modified 2011]
 
 
EC 2.4.1.192     
Accepted name: nuatigenin 3β-glucosyltransferase
Reaction: UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol = UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol 3-O-β-D-glucoside
Other name(s): uridine diphosphoglucose-nuatigenin glucosyltransferase
Systematic name: UDP-glucose:(20S,22S,25S)-22,25-epoxyfurost-5-ene-3β,26-diol 3-O-β-D-glucosyltransferase
Comments: Some other sapogenins can act as glucosyl acceptors. Involved in the biosynthesis of plant saponins. Not identical with EC 2.4.1.173 (sterol 3β-glucosyltransferase) or EC 2.4.1.193 (sarsapogenin 3β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 108891-57-2
References:
1.  Kalinowska, M. and Wojciechowski, Z.A. Enzymatic-synthesis of nuatigenin 3-β-D-glucoside in oat (Avena sativa) leaves. Phytochemistry 25 (1986) 2525–2529.
2.  Kalinowska, M. and Wojciechowski, Z.A. Subcellular-localization of UDPG-nuatigenin glucosyltransferase in oat leaves. Phytochemistry 26 (1987) 353–357.
[EC 2.4.1.192 created 1992]
 
 
EC 2.4.1.193     
Accepted name: sarsapogenin 3β-glucosyltransferase
Reaction: UDP-glucose + (25S)-5β-spirostan-3β-ol = UDP + (25S)-5β-spirostan-3β-ol 3-O-β-D-glucoside
Other name(s): uridine diphosphoglucose-sarsapogenin glucosyltransferase
Systematic name: UDP-glucose:(25S)-5β-spirostan-3β-ol 3-O-β-D-glucosyltransferase
Comments: Specific to 5β-spirostanols. Involved in the biosynthesis of plant saponins. Not identical with EC 2.4.1.173 (sterol 3β-glucosyltransferase) or EC 2.4.1.192 (nuatigenin 3β-glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117698-14-3
References:
1.  Paczkowski, C. and Wojciechowski, Z.A. The occurrence of UDPG-dependent glucosyltransferase specific for sarsasapogenin in Asparagus officinalis. Phytochemistry 27 (1988) 2743–2747.
[EC 2.4.1.193 created 1992]
 
 
EC 2.4.1.194     
Accepted name: 4-hydroxybenzoate 4-O-β-D-glucosyltransferase
Reaction: UDP-glucose + 4-hydroxybenzoate = UDP + 4-(β-D-glucosyloxy)benzoate
Other name(s): uridine diphosphoglucose-4-hydroxybenzoate glucosyltransferase; UDP-glucose:4-(β-D-glucopyranosyloxy)benzoic acid glucosyltransferase; HBA glucosyltransferase; p-hydroxybenzoate glucosyltransferase; PHB glucosyltransferase; PHB-O-glucosyltransferase
Systematic name: UDP-glucose:4-hydroxybenzoate 4-O-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120860-68-6
References:
1.  Katsumata, T., Shige, H. and Ejiri, S.-I. Biochemical-studies on pollen. 34. UDP glucose-4-(β-D-glucopyranosyloxy) benzoic-acid glucosyltransferase from the pollen of Pinus densiflora. Phytochemistry 28 (1989) 359–362.
[EC 2.4.1.194 created 1992]
 
 
EC 2.4.1.195     
Accepted name: N-hydroxythioamide S-β-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + (Z)-2-phenyl-1-thioacetohydroximate = UDP + desulfoglucotropeolin
(2) UDP-α-D-glucose + an (E)-ω-(methylsulfanyl)alkyl-thiohydroximate = UDP + an aliphatic desulfoglucosinolate
(3) UDP-α-D-glucose + (E)-2-(1H-indol-3-yl)-1-thioacetohydroximate = UDP + desulfoglucobrassicin
For diagram of glucotropeolin biosynthesis, click here
Glossary: an aliphatic desulfoglucosinolate = an ω-(methylsulfanyl)alkylhydroximate S-glucoside
Other name(s): UGT74B1 (gene name); desulfoglucosinolate-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-thiohydroximate glucosyltransferase; thiohydroximate β-D-glucosyltransferase; UDPG:thiohydroximate glucosyltransferase; thiohydroximate S-glucosyltransferase; thiohydroximate glucosyltransferase; UDP-glucose:thiohydroximate S-β-D-glucosyltransferase; UDP-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase
Comments: The enzyme specifically glucosylates the thiohydroximate functional group. It is involved in the biosynthesis of glucosinolates in cruciferous plants, and acts on aliphatic, aromatic, and indolic substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-14-8
References:
1.  Jain, J.C., Reed, D.W., Groot Wassink, J.W.D. and Underhill, E.W. A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species. Anal. Biochem. 178 (1989) 137–140. [DOI] [PMID: 2524977]
2.  Reed, D.W., Davin, L., Jain, J.C., Deluca, V., Nelson, L. and Underhill, E.W. Purification and properties of UDP-glucose:thiohydroximate glucosyltransferase from Brassica napus L. seedlings. Arch. Biochem. Biophys. 305 (1993) 526–532. [DOI] [PMID: 8373190]
3.  Marillia, E.F., MacPherson, J.M., Tsang, E.W., Van Audenhove, K., Keller, W.A. and GrootWassink, J.W. Molecular cloning of a Brassica napus thiohydroximate S-glucosyltransferase gene and its expression in Escherichia coli. Physiol. Plant. 113 (2001) 176–184. [PMID: 12060294]
4.  Fahey, J.W., Zalcmann, A.T. and Talalay, P. The chemical diversity and distribution of glucosinolates and isothiocyanates among plants. Phytochemistry 56 (2001) 5–51. [DOI] [PMID: 11198818]
5.  Grubb, C.D., Zipp, B.J., Ludwig-Muller, J., Masuno, M.N., Molinski, T.F. and Abel, S. Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate biosynthesis and auxin homeostasis. Plant J. 40 (2004) 893–908. [DOI] [PMID: 15584955]
[EC 2.4.1.195 created 1992, modified 2006, modified 2018]
 
 
EC 2.4.1.196     
Accepted name: nicotinate glucosyltransferase
Reaction: UDP-glucose + nicotinate = UDP + N-glucosylnicotinate
Other name(s): uridine diphosphoglucose-nicotinate N-glucosyltransferase; UDP-glucose:nicotinic acid-N-glucosyltransferase
Systematic name: UDP-glucose:nicotinate N-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120858-56-2
References:
1.  Upmeier, B., Thomzik, J.E. and Barz, W. Enzymatic studies on the reversible synthesis of nicotinic acid-N-glucoside in heterotrophic parsley cell suspension cultures. Z. Naturforsch. C: Biosci. 43 (1988) 835–842.
[EC 2.4.1.196 created 1992]
 
 
EC 2.4.1.197     
Accepted name: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase
Reaction: Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked α-(1→6) to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum
Other name(s): uridine diphosphoacetylglucosamine-oligosaccharide acetylglucosaminyltransferase; acetylglucosamine-oligosaccharide acetylglucosaminyltransferase; UDP-GlcNAc:oligosaccharide β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide 4-β-N-acetylglucosaminyltransferase
Comments: The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by α-1,3 and α-1,6 links.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123425-54-7
References:
1.  Sharkey, D.J. and Kornfeld, R. Identification of an N-acetylglucosaminyltransferase in Dictyostelium discoideum that transfers an "intersecting" N-acetylglucosamine residue to high mannose oligosaccharides. J. Biol. Chem. 264 (1989) 10411–10419. [PMID: 2525124]
[EC 2.4.1.197 created 1992]
 
 
EC 2.4.1.198     
Accepted name: phosphatidylinositol N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns
Other name(s): UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase; uridine diphosphoacetylglucosamine α1,6-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-α-D-glucosaminyl)transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-α-D-glucosaminyl)transferase (configuration-retaining)
Comments: Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 144388-35-2
References:
1.  Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168–11173. [PMID: 2525555]
2.  Watanabe, R., Inoue, N., Westfall, B., Taron, C.H., Orlean, P., Takeda, J. and Kinoshita, T. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H , PIG-C and GPI1. EMBO J. 17 (1998) 877–885. [DOI] [PMID: 9463366]
3.  Watanabe, R., Murakami, Y., Marmor, M.D., Inoue, N., Maeda, Y., Hino, J., Kangawa, K., Julius, M. and Kinoshita, T. Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 19 (2000) 4402–4411. [DOI] [PMID: 10944123]
[EC 2.4.1.198 created 1992, modified 2002]
 
 
EC 2.4.1.201     
Accepted name: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein]
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Other name(s): MGAT4C (gene name); N-acetylglucosaminyltransferase VI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI; uridine diphosphoacetylglucosamine-glycopeptide β-1→4-acetylglucosaminyltransferase VI; mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTVI; GlcNAc-T VI; UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→2)]-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in β1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by β linkages. No homologous enzyme appears to exist in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119699-68-2
References:
1.  Brockhausen, I., Hull, E., Hindsgaul, O., Schachter, H., Shah, R.N., Michnick, S.W. and Carver, J.P. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc β1-6 (GlcNAc β1-2)Man α-R (GlcNAc to Man) β-4-N-acetylglucosaminyltransferase VI. J. Biol. Chem. 264 (1989) 11211–11221. [PMID: 2525556]
2.  Taguchi, T., Ogawa, T., Inoue, S., Inoue, Y., Sakamoto, Y., Korekane, H. and Taniguchi, N. Purification and characterization of UDP-GlcNAc:GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man]-β1,4-N-acetylglucosaminyltransferase VI from hen oviduct. J. Biol. Chem. 275 (2000) 32598–32602. [DOI] [PMID: 10903319]
3.  Sakamoto, Y., Taguchi, T., Honke, K., Korekane, H., Watanabe, H., Tano, Y., Dohmae, N., Takio, K., Horii, A. and Taniguchi, N. Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcβ 1-6(GlcNAcβ 1-2)- manα 1-R[GlcNAc to man]β 1,4N-acetylglucosaminyltransferase VI. J. Biol. Chem. 275 (2000) 36029–36034. [DOI] [PMID: 10962001]
[EC 2.4.1.201 created 1992, modified 2001, modified 2018]
 
 
EC 2.4.1.202     
Accepted name: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
(2) UDP-α-D-glucose + 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = UDP + (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside
For diagram of benzoxazinone biosynthesis, click here
Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = DIMBOA
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIMBOA β-D-glucoside
Other name(s): uridine diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-glucosyltransferase; BX8; BX9; benzoxazinoid glucosyltransferase; DIMBOA glucosyltransferase
Systematic name: UDP-α-D-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-β-D-glucosyltransferase
Comments: The enzyme is involved in the detoxification of the benzoxazinoids DIBOA (2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one) and DIMBOA (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) which are stored as the respective non-toxic glucosides in the vacuoles in some plants, most commonly from the family of Poaceae (grasses). Benzoxazinoids are known to exhibit antimicrobial, antifeedant, and antiinsecticidal effects and are involved in the interaction of plants with other plants, insects, or microorganisms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-56-3
References:
1.  Bailey, B.A. and Larson, R.L. Hydroxamic acid glucosyltransferases from maize seedlings. Plant Physiol. 90 (1989) 1071–1076. [PMID: 16666853]
2.  von Rad, U., Huttl, R., Lottspeich, F., Gierl, A. and Frey, M. Two glucosyltransferases are involved in detoxification of benzoxazinoids in maize. Plant J. 28 (2001) 633–642. [DOI] [PMID: 11851909]
[EC 2.4.1.202 created 1992, modified 2012]
 
 
EC 2.4.1.203     
Accepted name: trans-zeatin O-β-D-glucosyltransferase
Reaction: UDP-glucose + trans-zeatin = UDP + O-β-D-glucosyl-trans-zeatin
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): zeatin O-β-D-glucosyltransferase; uridine diphosphoglucose-zeatin O-glucosyltransferase; zeatin O-glucosyltransferase
Systematic name: UDP-glucose:trans-zeatin O-β-D-glucosyltransferase
Comments: Unlike EC 2.4.1.215, cis-zeatin O-β-D-glucosyltransferase, UDP-D-xylose can also act as donor (cf. EC 2.4.2.40, zeatin O-β-D-xylosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123644-76-8
References:
1.  Dixon, S.C., Martin, R.C., Mok, R.C., Shaw, G. and Mok, D.W.S. Zeatin glycosylation enzymes in Phaseolus - isolation of O-glucosyltransferase from Phaseolus lunatus and comparison to O-xylosyltransferase from P. vulgaris. Plant Physiol. 90 (1989) 1316–1321. [PMID: 16666929]
[EC 2.4.1.203 created 1992, modified 2001]
 
 
EC 2.4.1.205     
Accepted name: galactogen 6β-galactosyltransferase
Reaction: UDP-α-D-galactose + galactogen = UDP + (1→6)-β-D-galactosylgalactogen
Other name(s): uridine diphosphogalactose-galactogen galactosyltransferase; 1,6-D-galactosyltransferase; β-(1-6)-D-galactosyltransferase; UDP-galactose:galactogen β-1,6-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:galactogen 6-β-D-galactosyltransferase
Comments: Galactogen from Helix pomatia is the most effective acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 88273-54-5
References:
1.  Goudsmit, E.M., Ketchum, P.A., Grossens, M.K. and Blake, D.A. Biosynthesis of galactogen: identification of a β-(1→6)-D-galactosyltransferase in Helix pomatia albumen glands. Biochim. Biophys. Acta 992 (1989) 289–297. [DOI] [PMID: 2505854]
[EC 2.4.1.205 created 1992]
 
 
EC 2.4.1.206     
Accepted name: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of lactotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): LA2 synthase; β1→3-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lactosylceramide β-acetylglucosaminyltransferase; lactosylceramide β-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-β-D-glucosylceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-80-8
References:
1.  Gottfries, J., Percy, A.K., Maansson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253–261. [DOI] [PMID: 1825612]
2.  Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1→3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649–15658. [PMID: 2960671]
3.  Percy, A.K., Gottfries, J., Vilbergsson, G., Maansson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461–1465. [DOI] [PMID: 1901591]
[EC 2.4.1.206 created 1992]
 
 
EC 2.4.1.208     
Accepted name: diglucosyl diacylglycerol synthase (1,2-linking)
Reaction: UDP-α-D-glucose + 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[α-D-glucopyranosyl-(1→2)-O-α-D-glucopyranosyl]-sn-glycerol + UDP
Other name(s): monoglucosyl diacylglycerol (1→2) glucosyltransferase; MGlcDAG (1→2) glucosyltransferase; DGlcDAG synthase (ambiguous); UDP-glucose:1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol (1→2) glucosyltransferase; diglucosyl diacylglycerol synthase
Systematic name: UDP-α-D-glucose:1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol 2-glucosyltransferase
Comments: The enzyme from Acholeplasma laidlawii requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 168680-19-1
References:
1.  Karlsson, O.P., Rytomaa, M., Dahlqvist, A., Kinnunen, P.K., Wieslander, A. Correlation between bilayer lipid dynamics and activity of the diglucosyldiacylglycerol synthase from Acholeplasma laidlawii membranes. Biochemistry 35 (1996) 10094–10102. [DOI] [PMID: 8756472]
[EC 2.4.1.208 created 1999, modified 2014]
 
 
EC 2.4.1.209     
Accepted name: cis-p-coumarate glucosyltransferase
Reaction: UDP-glucose + cis-p-coumarate = 4′-O-β-D-glucosyl-cis-p-coumarate + UDP
Systematic name: UDP-glucose:cis-p-coumarate β-D-glucosyltransferase
Comments: cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr. The corresponding trans-isomers are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 196887-88-4
References:
1.  Rasmussen, S. and Rudolph, H. Isolation, purification and characterization of UDP-glucose:cis-p-coumaric acid-β-D-glucosyltransferase from Sphagnum fallax. Phytochemistry 46 (1997) 449–453.
[EC 2.4.1.209 created 2000]
 
 
EC 2.4.1.210     
Accepted name: limonoid glucosyltransferase
Reaction: UDP-glucose + limonin = glucosyl-limonin + UDP
Other name(s): uridine diphosphoglucose-limonoid glucosyltransferase
Systematic name: UDP-glucose:limonin glucosyltransferase
Comments: The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 195836-82-9
References:
1.  Shin, H., Suhayda, C.G., Hsu, W.-J. and Robertson, G.H. Purification of limonoid glucosyltransferase from navel orange albedo tissue. Phytochemistry 46 (1997) 33–37.
[EC 2.4.1.210 created 2000]
 
 
EC 2.4.1.212     
Accepted name: hyaluronan synthase
Reaction: (1) UDP-N-acetyl-α-D-glucosamine + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] = UDP + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan]
(2) UDP-α-D-glucuronate + N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan] = UDP + β-D-glucuronosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-[nascent hyaluronan]
For diagram of reaction, click here
Glossary: GlcA = glucuronic acid
Other name(s): spHAS; seHAS; Alternating UDP-α-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase
Systematic name: Alternating UDP-N-acetyl-α-D-glucosamine:β-D-glucuronosyl-(1→3)-[nascent hyaluronan] 4-N-acetyl-β-D-glucosaminyltransferase and UDP-α-D-glucuronate:N-acetyl-β-D-glucosaminyl-(1→4)-[nascent hyaluronan] 3-β-D-glucuronosyltransferase (configuration-inverting)
Comments: The enzyme from Streptococcus Group A and Group C requires Mg2+. The enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc [3]. The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in a variety of organisms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39346-43-5
References:
1.  DeAngelis, P.L., Papaconstantinou, J. and Weigel, P.H. Molecular cloning, identification and sequence of the hyaluronan synthase gene from Group A Streptococcus pyogenes. J. Biol. Chem. 268 (1993) 19181–19184. [PMID: 8366070]
2.  Jing, W. and DeAngelis, P.L. Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide. Glycobiology 10 (2000) 883–889. [DOI] [PMID: 10988250]
3.  DeAngelis, P.L. Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 274 (1999) 26557–26562. [DOI] [PMID: 10473619]
4.  Tlapak-Simmons, V.L., Baron, C.A. and Weigel, P.H. Characterization of the purified hyaluronan synthase from Streptococcus equisimilis. Biochemistry 43 (2004) 9234–9242. [DOI] [PMID: 15248781]
[EC 2.4.1.212 created 2001, modified 2007]
 
 
EC 2.4.1.215     
Accepted name: cis-zeatin O-β-D-glucosyltransferase
Reaction: UDP-glucose + cis-zeatin = UDP + O-β-D-glucosyl-cis-zeatin
Glossary: zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
Systematic name: UDP-glucose:cis-zeatin O-β-D-glucosyltransferase
Comments: The enzyme from maize can use cis-zeatin and UDP-glucose as substrates, but not cis-ribosylzeatin, trans-zeatin or trans-ribosylzeatin. Unlike EC 2.4.1.203, trans-zeatin O-β-D-glucosyltransferase, UDP-D-xylose cannot act as a donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123644-76-8
References:
1.  Martin, R.C., Mok, M.C., Habben, J.E. and Mok, D.W.S. A maize cytokinin gene encoding an O-glucosyltransferase specific to cis-zeatin. Proc. Natl. Acad. Sci. USA 98 (2001) 5922–5926. [DOI] [PMID: 11331778]
[EC 2.4.1.215 created 2001]
 
 
EC 2.4.1.218     
Accepted name: hydroquinone glucosyltransferase
Reaction: UDP-glucose + hydroquinone = UDP + hydroquinone-O-β-D-glucopyranoside
Other name(s): arbutin synthase; hydroquinone:O-glucosyltransferase
Systematic name: UDP-glucose:hydroquinone-O-β-D-glucosyltransferase
Comments: Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Arend, J., Warzecha, H. and Stöckigt, J. Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences. Phytochemistry 53 (2000) 187–193. [DOI] [PMID: 10680170]
2.  Arend, J., Warzecha, H., Hefner, T. and Stöckigt, J. Utilizing genetically engineered bacteria to produce plant specific glucosides. Biotechnol. Bioeng. 76 (2001) 126–131. [PMID: 11505382]
[EC 2.4.1.218 created 2002]
 
 
EC 2.4.1.219     
Accepted name: vomilenine glucosyltransferase
Reaction: UDP-glucose + vomilenine = UDP + raucaffricine
For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here
Other name(s): UDPG:vomilenine 21-β-D-glucosyltransferase
Systematic name: UDP-glucose:vomilenine 21-O-β-D-glucosyltransferase
Comments: The indole alkaloid raucaffricine accumulates during the culture of Rauvolfia cell suspensions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Warzecha, H., Obitz, P. and Stöckigt, J. Purification, partial amino acid sequence and structure of the product of raucaffricine-O-β-D-glucosidase from plant cell cultures of Rauwolfia serpentina. Phytochemistry 50 (1999) 1099–1109. [DOI] [PMID: 10234858]
2.  Warzecha, H., Gerasimenko, I., Kutchan, T.M. and Stöckigt, J. Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis. Phytochemistry 54 (2000) 657–666. [DOI] [PMID: 10975500]
3.  Ruyter, C.M. and Stöckigt, J. Enzymatic formation of raucaffricine, the major indole alkaloid of Rauwolfia serpentina cell-suspension cultures. Helv. Chim. Acta 74 (1991) 1707–1712.
[EC 2.4.1.219 created 2002]
 
 
EC 2.4.1.220     
Accepted name: indoxyl-UDPG glucosyltransferase
Reaction: UDP-glucose + indoxyl = UDP + indican
Glossary: indoxyl = indole-3-ol
Other name(s): indoxyl-UDPG-glucosyltransferase
Systematic name: UDP-glucose:indoxyl 3-O-β-D-glucosyltransferase
Comments: Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole. After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 258339-72-9
References:
1.  Marcinek, H., Weyler, W., Deus-Neumann, B. and Zenk, M.H. Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia. Phytochemistry 53 (2000) 201–207. [DOI] [PMID: 10680172]
[EC 2.4.1.220 created 2002]
 
 
EC 2.4.1.222     
Accepted name: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) = UDP + [protein with EGF-like domain]-3-O-[N-acetyl-β-D-glucosaminyl-(1→3)-α-L-fucosyl]-(L-serine/L-threonine)
Glossary: EGF = epidermal growth factor
EGF-like domain = an evolutionary conserved domain containing 30 to 40 amino-acid residues first described from epidermal growth factor
Other name(s): O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase; fringe; UDP-D-GlcNAc:O-L-fucosylpeptide 3-β-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein with EGF-like domain]-3-O-(α-L-fucosyl)-(L-serine/L-threonine) 3-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Comments: The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc and α-Neu5Ac-(2→6)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-α-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 299203-70-6
References:
1.  Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. and Vogt, T.F. Fringe is a glycosyltransferase that modifies Notch. Nature 406 (2000) 369–375. [DOI] [PMID: 10935626]
2.  Bruckner, K., Perez, L., Clausen, H. and Cohen, S. Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406 (2000) 411–415. [DOI] [PMID: 10935637]
3.  Rampal, R., Li, A.S., Moloney, D.J., Georgiou, S.A., Luther, K.B., Nita-Lazar, A. and Haltiwanger, R.S. Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeats. J. Biol. Chem. 280 (2005) 42454–42463. [DOI] [PMID: 16221665]
[EC 2.4.1.222 created 2002, modified 2022]
 
 
EC 2.4.1.223     
Accepted name: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(α-D-GlcNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of heparan biosynthesis (later stages), click here
Glossary: [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
Other name(s): α-N-acetylglucosaminyltransferase I; α1,4-N-acetylglucosaminyltransferase; glucuronosylgalactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl-proteoglycan 4IV-α-N-acetyl-D-glucosaminyltransferase; glucuronyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4IV-α-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Comments: Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. Apparently products of both the human EXTL2 and EXTL3 genes can catalyse this reaction. In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224, glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. For explanation of the use of a superscript in the systematic name, see 2-Carb-37.2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 179241-74-8
References:
1.  Kitagawa, H., Shimakawa, H. and Sugahara, K. The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274 (1999) 13933–13937. [DOI] [PMID: 10318803]
2.  Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834–4838. [DOI] [PMID: 11121397]
[EC 2.4.1.223 created 2002, modified 2016]
 
 
EC 2.4.1.224     
Accepted name: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-D-glucosamine + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan = UDP + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan
For diagram of heparan biosynthesis (later stages), click here
Other name(s): α-N-acetylglucosaminyltransferase II glucuronyl-N-acetylglucosaminylproteoglycan α-1,4-N-acetylglucosaminyltransferase
Systematic name: UDP-N-acetyl-D-glucosamine:β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase
Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the 4-β-glucuronosyltransferase (EC 2.4.1.225, N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase) activity required for the synthesis of the heparan sulfate disaccharide repeats. Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-α-N-acetylglucosaminyltransferase activity. In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223, glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 336193-98-7
References:
1.  Kim, B.T., Kitagawa, H., Tamura, J., Saito, T., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode α1,4-N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/heparin biosynthesis. Proc. Natl. Acad. Sci. USA 98 (2001) 7176–7181. [DOI] [PMID: 11390981]
2.  Kitagawa, H., Egusa, N., Tamura, J.I., Kusche-Gullberg, M., Lindahl, U. and Sugahara, K. rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel α1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate. J. Biol. Chem. 276 (2001) 4834–4838. [DOI] [PMID: 11121397]
3.  Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282–286. [DOI] [PMID: 11256613]
4.  Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265–26268. [DOI] [PMID: 9756849]
[EC 2.4.1.224 created 2002]
 
 
EC 2.4.1.225     
Accepted name: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase
Reaction: UDP-α-D-glucuronate + N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan = UDP + β-D-glucuronosyl-(1→4)-N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan
For diagram of the later stages of heparan biosynthesis, click here
Other name(s): N-acetylglucosaminylproteoglycan β-1,4-glucuronyltransferase; heparan glucuronyltransferase II
Systematic name: UDP-α-D-glucuronate:N-acetyl-α-D-glucosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 4-β-glucuronosyltransferase
Comments: Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 145539-84-0
References:
1.  Senay, C., Lind, T., Muguruma, K., Tone, Y., Kitagawa, H., Sugahara, K., Lidholt, K., Lindahl, U. and Kusche-Gullberg, M. The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis. EMBO Rep. 1 (2000) 282–286. [DOI] [PMID: 11256613]
2.  Lind, T., Tufaro, F., McCormick, C., Lindahl, U. and Lidholt, K. The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273 (1998) 26265–26268. [DOI] [PMID: 9756849]
[EC 2.4.1.225 created 2002]
 
 
EC 2.4.1.226     
Accepted name: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase
Reaction: (1) UDP-α-D-glucuronate + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
(2) UDP-α-D-glucuronate + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine
For diagram of chondroitin biosynthesis (later stages), click here
Other name(s): chondroitin glucuronyltransferase II; α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase; UDP-α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase
Systematic name: UDP-α-D-glucuronate:[protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 3-β-glucuronosyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 269077-98-7
References:
1.  Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575]
2.  DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104]
3.  Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778]
4.  Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine. J. Biol. Chem. 277 (2002) 38179–38188. [DOI] [PMID: 12145278]
[EC 2.4.1.226 created 2002, modified 2018]
 
 
EC 2.4.1.227     
Accepted name: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
For diagram of peptidoglycan biosynthesis (part 2), click here
Other name(s): MurG transferase; UDP-N-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase (configuration-inverting)
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60976-26-3
References:
1.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 2.4.1.227 created 2002]
 
 
EC 2.4.1.228     
Accepted name: lactosylceramide 4-α-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of globotetraosylceramide biosynthesis, click here
Glossary: lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
Other name(s): Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose; UDP-galactose:lactosylceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl(1↔1)ceramide 4II-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-galactosyl-(1→4)-D-glucosyl-(1↔1)-ceramide 4II-α-D-galactosyltransferase
Comments: For explanation of superscript II in systematic name, see 2-carb.37.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52725-57-2
References:
1.  Bailly, P., Piller, F., Cartron, J.P., Leroy, Y. and Fournet, B. Identification of UDP-galactose: lactose (lactosylceramide) α-4 and β-3 galactosyltransferases in human kidney. Biochem. Biophys. Res. Commun. 141 (1986) 84–91. [DOI] [PMID: 3099784]
2.  Steffensen, R., Carlier, K., Wiels, J., Levery, S.B., Stroud, M., Cedergren, B., Nilsson Sojka, B., Bennett, E.P., Jersild, C. and Clausen, H. Cloning and expression of the histo-blood group Pk UDP-galactose: Galβ1-4Glcβ1-Cer α1,4-galactosyltransferase. Molecular genetic basis of the p phenotype. J. Biol. Chem. 275 (2000) 16723–16729. [DOI] [PMID: 10747952]
3.  Kojima, Y., Fukumoto, S., Furukawa, K., Okajima, T., Wiels, J., Yokoyama, K., Suzuki, Y., Urano, T., Ohta, M. and Furukawa, K. Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J. Biol. Chem. 275 (2000) 15152–15156. [DOI] [PMID: 10748143]
[EC 2.4.1.228 created 2002]
 
 
EC 2.4.1.229     
Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline
Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase
Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 256531-81-4
References:
1.  van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [DOI] [PMID: 12244115]
2.  Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [DOI] [PMID: 10593934]
3.  West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [DOI] [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 
EC 2.4.1.234     
Accepted name: kaempferol 3-O-galactosyltransferase
Reaction: UDP-α-D-galactose + kaempferol = UDP + kaempferol 3-O-β-D-galactoside
For diagram of kaempferol biosynthesis, click here
Other name(s): F3GalTase; UDP-galactose:kaempferol 3-O-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:kaempferol 3-O-β-D-galactosyltransferase
Comments: Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin. The reaction can occur equally well in both directions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miller, K.D., Guyon, V., Evans, J.N., Shuttleworth, W.A. and Taylor, L.P. Purification, cloning, and heterologous expression of a catalytically efficient flavonol 3-O-galactosyltransferase expressed in the male gametophyte of Petunia hybrida. J. Biol. Chem. 274 (1999) 34011–34019. [DOI] [PMID: 10567367]
[EC 2.4.1.234 created 2004]
 
 
EC 2.4.1.235      
Deleted entry: cyanidin 3-O-rutinoside 5-O-glucosyltransferase. Enzyme is identical to EC 2.4.1.116, cyanidin 3-O-rutinoside 5-O-glucosyltransferase
[EC 2.4.1.235 created 2004, deleted 2006]
 
 
EC 2.4.1.236     
Accepted name: flavanone 7-O-glucoside 2′′-O-β-L-rhamnosyltransferase
Reaction: UDP-β-L-rhamnose + a flavanone 7-O-β-D-glucoside = UDP + a flavanone 7-O-[α-L-rhamnosyl-(1→2)-β-D-glucoside]
For diagram of apigenin derivatives biosynthesis, click here, for diagram of luteolin derivatives biosynthesis, click here and for diagram of naringenin derivatives biosynthesis, click here
Glossary: UDP-β-L-rhamnose = UDP-6-deoxy-β-L-mannose
Other name(s): UDP-rhamnose:flavanone-7-O-glucoside-2′′-O-rhamnosyltransferase; 1→2 UDP-rhamnosyltransferase; UDP-L-rhamnose:flavanone-7-O-glucoside 2′′-O-β-L-rhamnosyltransferase
Systematic name: UDP-β-L-rhamnose:flavanone-7-O-glucoside 2′′-O-α-L-rhamnosyltransferase
Comments: Acts on the 7-O-glucoside of naringenin and hesperetin, also the flavone 7-O-glucosides of luteolin and apigenin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-89-8
References:
1.  Bar-Peled, M., Lewinsohn, E., Fluhr, R. and Gressel, J. UDP-rhamnose:flavanone-7-O-glucoside-2′′-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus. J. Biol. Chem. 266 (1991) 20953–20959. [PMID: 1939145]
[EC 2.4.1.236 created 2004]
 
 
EC 2.4.1.237     
Accepted name: flavonol 7-O-β-glucosyltransferase
Reaction: UDP-glucose + a flavonol = UDP + a flavonol 7-O-β-D-glucoside
For diagram of quercetin 7-O-Glycoside biosynthesis, click here
Other name(s): UDP-glucose:flavonol 7-O-glucosyltransferase
Systematic name: UDP-glucose:flavonol 7-O-β-D-glucosyltransferase
Comments: Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a lesser extent on quercetin, kaempferol and myricetin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-90-0
References:
1.  Stich, K., Halbwirth, H., Wurst, F. and Forkmann, G. UDP-glucose: flavonol 7-O-glucosyltransferase activity in flower extracts of Chrysanthemum segetum. Z. Naturforsch. C 52 (1997) 153–158. [PMID: 9167271]
[EC 2.4.1.237 created 2004]
 
 
EC 2.4.1.238     
Accepted name: delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase
Reaction: UDP-α-D-glucose + delphinidin 3,5-di-O-β-D-glucoside = UDP + delphinidin 3,3′,5-tri-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
Other name(s): UDP-glucose:anthocyanin 3′-O-glucosyltransferase; 3’GT
Systematic name: UDP-α-D-glucose:delphinidin-3,5-di-O-β-D-glucoside 3′-O-glucosyltransferase
Comments: Isolated from the plant Gentiana triflora (clustered gentian).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 380231-41-4
References:
1.  Fukuchi-Mizutani, M., Okuhara, H., Fukui, Y., Nakao, M., Katsumoto, Y., Yonekura-Sakakibara, K., Kusumi, T., Hase, T. and Tanaka, Y. Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3′-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian. Plant Physiol. 132 (2003) 1652–1663. [DOI] [PMID: 12857844]
[EC 2.4.1.238 created 2004, modified 2013]
 
 
EC 2.4.1.239     
Accepted name: flavonol-3-O-glucoside glucosyltransferase
Reaction: UDP-glucose + a flavonol 3-O-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside
For diagram of kaempferol-glycoside biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-triglucoside, click here
Other name(s): UDP-glucose:flavonol-3-O-glucoside 2′′-O-β-D-glucosyltransferase
Systematic name: UDP-glucose:flavonol-3-O-β-D-glucoside 2′′-O-β-D-glucosyltransferase
Comments: One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240, flavonol-3-O-glycoside glucosyltransferase). TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434–443. [DOI] [PMID: 6462109]
[EC 2.4.1.239 created 2004]
 
 
EC 2.4.1.240     
Accepted name: flavonol-3-O-glycoside glucosyltransferase
Reaction: UDP-glucose + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucoside = UDP + a flavonol 3-O-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside
For diagram of kaempferol-glycoside biosynthesis, click here and for diagram of the biosynthesis of quercetin 3-O-triglucoside, click here
Systematic name: UDP-glucose:flavonol-3-O-β-D-glucosyl-(1→2)-β-D-glucoside 2′′′-O-β-D-glucosyltransferase
Comments: One of three specific glucosyltransferases in pea (Pisum sativum) thatsuccessively add a β-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jourdan, P.S. and Mansell, R.L. Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. Arch. Biochem. Biophys. 213 (1982) 434–443. [DOI] [PMID: 6462109]
[EC 2.4.1.240 created 2004]
 
 
EC 2.4.1.241     
Accepted name: digalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase; UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol 6-α-galactosyltransferase
Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC 2.4.1.46, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 69913-00-4
References:
1.  Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166–1173. [DOI] [PMID: 11696551]
2.  Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649–10654. [DOI] [PMID: 10973486]
3.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC 2.4.1.241 created 2005]
 
 
EC 2.4.1.242     
Accepted name: NDP-glucose—starch glucosyltransferase
Reaction: NDP-glucose + [(1→4)-α-D-glucosyl]n = NDP + [(1→4)-α-D-glucosyl]n+1
Other name(s): granule-bound starch synthase; starch synthase II (ambiguous); waxy protein; starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase; granule-bound starch synthase I; GBSSI; granule-bound starch synthase II; GBSSII; GBSS; NDPglucose-starch glucosyltransferase
Systematic name: NDP-glucose:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Comments: Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-53-2
References:
1.  Tsai, C.-Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11 (1974) 83–96. [PMID: 4824506]
2.  Nakamura, T., Vrinten, P., Hayakawa, K. and Ikeda, J. Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 118 (1998) 451–459. [PMID: 9765530]
3.  Fujita, N. and Taira, T. A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 207 (1998) 125–132. [DOI] [PMID: 9951718]
4.  Murai, J., Taira, T. and Ohta, D. Isolation and characterization of the three Waxy genes encoding the granule-bound starch synthase in hexaploid wheat. Gene 234 (1999) 71–79. [DOI] [PMID: 10393240]
5.  Nelson, O.E. The waxy locus in maize. II The location of the controlling element alleles. Genetics 60 (1968) 507–524. [PMID: 17248421]
[EC 2.4.1.242 created 2005]
 
 
EC 2.4.1.244     
Accepted name: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group
Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosamine = N,N′-diacetyllactosediamine
Other name(s): β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase
Comments: The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534–47544. [DOI] [PMID: 12966086]
2.  Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of β1,4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134–140. [DOI] [PMID: 15044014]
[EC 2.4.1.244 created 2006]
 
 
EC 2.4.1.245     
Accepted name: α,α-trehalose synthase
Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP
Glossary: NDP = a nucleoside diphosphate
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-α-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [DOI] [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [DOI] [PMID: 15737605]
3.  Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939–7946. [DOI] [PMID: 18835983]
4.  Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355–369. [DOI] [PMID: 18483808]
[EC 2.4.1.245 created 2008, modified 2013]
 
 
EC 2.4.1.249     
Accepted name: delphinidin 3′,5′-O-glucosyltransferase
Reaction: 2 UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = 2 UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside (overall reaction)
(1a) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside
(1b) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside
For diagram of anthocyanidin acylglucoside biosynthesis, click here
Glossary: delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside = ternatin C5
Other name(s): UDP-glucose:anthocyanin 3′,5′-O-glucosyltransferase; UA3′5’GZ
Systematic name: UDP-glucose:delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside 3′-O-glucosyltransferase
Comments: Ternatins are a group of polyacetylated delphinidin glucosides that confer blue color to the petals of Clitoria ternatea (butterfly pea). This enzyme catalyses two reactions in the biosynthesis of ternatin C5: the conversion of delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside to delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside, followed by the conversion of the later to ternatin C5, by transferring two glucosyl groups in a stepwise manner [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kogawa, K., Kato, N., Kazuma, K., Noda, N. and Suzuki, M. Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase from Clitoria ternatea. Planta 226 (2007) 1501–1509. [DOI] [PMID: 17668234]
[EC 2.4.1.249 created 2009]
 
 
EC 2.4.1.250     
Accepted name: D-inositol-3-phosphate glycosyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP
For diagram of mycothiol biosynthesis, click here
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
Other name(s): mycothiol glycosyltransferases; MshA; UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase (configuration-retaining)
Comments: The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476–3479. [DOI] [PMID: 12754249]
2.  Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910–33920. [DOI] [PMID: 16940050]
3.  Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834–15844. [DOI] [PMID: 18390549]
[EC 2.4.1.250 created 2010]
 
 
EC 2.4.1.253     
Accepted name: baicalein 7-O-glucuronosyltransferase
Reaction: UDP-D-glucuronate + baicalein = UDP + baicalin
Glossary: baicalin = 5,6,7-trihydroxyflavone-7-O-β-D-glucuronate = 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl β-D-glucupyranosiduronic acid
baicalein = 5,6,7-trihydroxyflavone = 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one
wogonin = 5,7-dihydroxy-8-methoxyflavone = 5,7-dihydroxy-8-methoxy-2-phenyl-4H-chromen-4-one
scutellarein = 4,5,6,7-tetrahydroxyflavone-7-O-β-D-glucoronate = 5,6,7-trihydroxy-2-(4-hydroxyphenyl)chromen-4-one
Other name(s): UBGAT
Systematic name: UDP-D-glucuronate:5,6,7-trihydroxyflavone 7-O-glucuronosyltransferase
Comments: The enzyme is specific for UDP-D-glucuronate as a sugar donor and flavones with substitution ortho- to the 7-OH group such as baicalein (6-OH), scutellarein (6-OH) and wogonin (8-OMe).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nagashima, S., Hirotani, M. and Yoshikawa, T. Purification and characterization of UDP-glucuronate: baicalein 7-O-glucuronosyltransferase from Scutellaria baicalensis Georgi. cell suspension cultures. Phytochemistry 53 (2000) 533–538. [DOI] [PMID: 10724177]
[EC 2.4.1.253 created 2011]
 
 


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