The Enzyme Database

Your query returned 15 entries.    printer_iconPrintable version



EC 2.4.1.168     
Accepted name: xyloglucan 4-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a β-(1→4)-D-glucosyl-D-glucose linkage
Other name(s): uridine diphosphoglucose-xyloglucan 4β-glucosyltransferase; xyloglucan 4β-D-glucosyltransferase; xyloglucan glucosyltransferase; UDP-glucose:xyloglucan 1,4-β-D-glucosyltransferase
Systematic name: UDP-glucose:xyloglucan 4-β-D-glucosyltransferase
Comments: In association with EC 2.4.2.39 (xyloglucan 6-xylosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are essential for this synthesis. Not identical with EC 2.4.1.12 cellulose synthase (UDP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80237-91-8
References:
1.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117–11122. [PMID: 6457048]
2.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells - synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517–523.
[EC 2.4.1.168 created 1989]
 
 
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 2.4.2.26     
Accepted name: protein xylosyltransferase
Reaction: UDP-α-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(β-D-xylosyl)-L-serine
For diagram of heparan and chondroitin biosynthesis (early stages), click here
Other name(s): UDP-D-xylose:core protein β-D-xylosyltransferase; UDP-D-xylose:core protein xylosyltransferase; UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase; UDP-xylose-core protein β-D-xylosyltransferase; uridine diphosphoxylose-core protein β-xylosyltransferase; uridine diphosphoxylose-protein xylosyltransferase; UDP-D-xylose:protein β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:protein β-D-xylosyltransferase (configuration-inverting)
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55576-38-0
References:
1.  Stoolmiller, A.C., Horwitz, A.L. and Dorfman, A. Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase. J. Biol. Chem. 247 (1972) 3525–3532. [PMID: 5030630]
2.  Götting, C., Kuhn, J., Zahn, R., Brinkmann, T. and Kleesiek, K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J. Mol. Biol. 304 (2000) 517–528. [DOI] [PMID: 11099377]
[EC 2.4.2.26 created 1976, modified 2002, modified 2016]
 
 
EC 2.4.2.39     
Accepted name: xyloglucan 6-xylosyltransferase
Reaction: Transfers an α-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an α-(1→6)-D-xylosyl-D-glucose linkage
Other name(s): uridine diphosphoxylose-xyloglucan 6α-xylosyltransferase; xyloglucan 6-α-D-xylosyltransferase; UDP-D-xylose:xyloglucan 1,6-α-D-xylosyltransferase
Systematic name: UDP-D-xylose:xyloglucan 6-α-D-xylosyltransferase
Comments: In association with EC 2.4.1.168 (xyloglucan 4-glucosyltransferase), this enzyme brings about the synthesis of xyloglucan; concurrent transfers of glucose and xylose are necessary for this synthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80238-01-3
References:
1.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells. Occurrence and some properties of xyloglucan 4-β-D-glucosyltransferase and 6-α-D-xylosyltransferase. J. Biol. Chem. 256 (1981) 11117–11122. [PMID: 6457048]
2.  Hayashi, T. and Matsuda, K. Biosynthesis of xyloglucan in suspension-cultured soybean cells - synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant Cell Physiol. 22 (1981) 517–523.
[EC 2.4.2.39 created 1989 as EC 2.4.1.169, transferred 2003 to EC 2.4.2.39]
 
 
EC 2.7.1.46     
Accepted name: L-arabinokinase
Reaction: ATP + L-arabinose = ADP + β-L-arabinose 1-phosphate
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): L-arabinokinase (phosphorylating)
Systematic name: ATP:L-arabinose 1-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-99-9
References:
1.  Neufeld, E.F., Feingold, D.S. and Hassid, W.Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 906–909. [PMID: 14426659]
[EC 2.7.1.46 created 1965]
 
 
EC 2.7.7.11     
Accepted name: UTP—xylose-1-phosphate uridylyltransferase
Reaction: UTP + α-D-xylose 1-phosphate = diphosphate + UDP-xylose
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): xylose-1-phosphate uridylyltransferase; uridylyltransferase, xylose 1-phosphate; UDP-xylose pyrophosphorylase; uridine diphosphoxylose pyrophosphorylase; xylose 1-phosphate uridylyltransferase
Systematic name: UTP:α-D-xylose-1-phosphate uridylyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-20-4
References:
1.  Ginsburg, V., Neufeld, E.F. and Hassid, W.Z. Enzymatic synthesis of uridine diphosphate xylose and uridine diphosphate arabinose. Proc. Natl. Acad. Sci. USA 42 (1956) 333–335. [DOI] [PMID: 16578456]
[EC 2.7.7.11 created 1961]
 
 
EC 2.7.7.37     
Accepted name: aldose-1-phosphate nucleotidyltransferase
Reaction: NDP + α-D-aldose 1-phosphate = phosphate + NDP-aldose
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): sugar-1-phosphate nucleotidyltransferase; NDPaldose phosphorylase; glucose 1-phosphate inosityltransferase; NDP sugar phosphorylase; nucleoside diphosphosugar phosphorylase; sugar phosphate nucleotidyltransferase; nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase; sugar nucleotide phosphorylase; NDP:aldose-1-phosphate nucleotidyltransferase
Systematic name: NDP:α-D-aldose-1-phosphate nucleotidyltransferase
Comments: The enzyme works on a variety of α-D-aldose 1-phosphates and β-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-61-8
References:
1.  Cabib, E., Carminatti, H. and Woyskovsky, N.M. Phosphorolysis of the pyrophosphate bond of sugar nucleotides. II. Purification and properties of the enzyme. J. Biol. Chem. 240 (1965) 2114–2121. [PMID: 14299635]
[EC 2.7.7.37 created 1972, modified 1986]
 
 
EC 2.7.7.44     
Accepted name: glucuronate-1-phosphate uridylyltransferase
Reaction: UTP + 1-phospho-α-D-glucuronate = diphosphate + UDP-α-D-glucuronate
For diagram of UDP-L-arabinose, UDP-galacturonate and UDP-xylose biosynthesis, click here
Other name(s): UDP-glucuronate pyrophosphorylase; UDP-D-glucuronic acid pyrophosphorylase; UDP-glucuronic acid pyrophosphorylase; uridine diphosphoglucuronic pyrophosphorylase
Systematic name: UTP:1-phospho-α-D-glucuronate uridylyltransferase
Comments: Also acts slowly with CTP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 52228-05-4
References:
1.  Roberts, R.M. The formation of uridine diphosphate-glucuronic acid in plants. Uridine diphosphate-glucuronic acid pyrophosphorylase from barley seedlings. J. Biol. Chem. 246 (1971) 4995–5002. [PMID: 5570433]
[EC 2.7.7.44 created 1976]
 
 
EC 2.7.7.64     
Accepted name: UTP-monosaccharide-1-phosphate uridylyltransferase
Reaction: UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide
Glossary: UDP-Xyl = UDP-α-D-xylose
UDP-L-Ara = UDP-β-L-arabinopyranose
Other name(s): UDP-sugar pyrophosphorylase; PsUSP
Comments: Requires Mg2+ or Mn2+ for maximal activity. The reaction can occur in either direction and it has been postulated that MgUTP and Mg-diphosphate are the actual substrates [1,2]. The enzyme catalyses the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl, showing broad substrate specificity towards monosaccharide 1-phosphates. Mannose 1-phosphate, L-Fucose 1-phosphate and glucose 6-phosphate are not substrates and UTP cannot be replaced by other nucleotide triphosphates [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kotake, T., Yamaguchi, D., Ohzono, H., Hojo, S., Kaneko, S., Ishida, H.K. and Tsumuraya, Y. UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts. J. Biol. Chem. 279 (2004) 45728–45736. [DOI] [PMID: 15326166]
2.  Rudick, V.L. and Weisman, R.A. Uridine diphosphate glucose pyrophosphorylase of Acanthamoeba castellanii. Purification, kinetic, and developmental studies. J. Biol. Chem. 249 (1974) 7832–7840. [PMID: 4430676]
[EC 2.7.7.64 created 2006]
 
 
EC 2.7.8.32     
Accepted name: 3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase
Reaction: UDP-xylose + 3-O-α-D-mannopyranosyl-α-D-mannopyranose = UMP + 3-O-(6-O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose
Glossary: O-α-D-xylosylphospho-α-D-mannopyranosyl)-α-D-mannopyranose = O-α-D-xylosylphosphono-α-D-mannopyranosyl)-α-D-mannopyranose
Other name(s): XPT1
Systematic name: UDP-D-xylose:3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase
Comments: Mn2+ required for activity. The enzyme is specific for mannose as an acceptor but is flexible as to the structural context of the mannosyl disaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Reilly, M.C., Levery, S.B., Castle, S.A., Klutts, J.S. and Doering, T.L. A novel xylosylphosphotransferase activity discovered in Cryptococcus neoformans. J. Biol. Chem. 284 (2009) 36118–36127. [DOI] [PMID: 19864415]
[EC 2.7.8.32 created 2011]
 
 
EC 4.1.1.35     
Accepted name: UDP-glucuronate decarboxylase
Reaction: UDP-D-glucuronate = UDP-D-xylose + CO2
For diagram of the biosynthesis of UDP-L-arabinose, UDP-galacturonate and UDP-xylose, click here
Other name(s): uridine-diphosphoglucuronate decarboxylase; UDP-D-glucuronate carboxy-lyase
Systematic name: UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming)
Comments: Requires NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-68-4
References:
1.  Ankel, H. and Feingold, D.S. Biosynthesis of uridine diphosphate D-xylose. 1. Uridine diphosphate glucuronate carboxy-lyase of wheat germ. Biochemistry 4 (1965) 2468–2475.
[EC 4.1.1.35 created 1965]
 
 
EC 4.1.1.67     
Accepted name: UDP-galacturonate decarboxylase
Reaction: UDP-D-galacturonate = UDP-L-arabinose + CO2
For diagram of the biosynthesis of UDP-L-arabinose, UDP-galacturonate and UDP-xylose, click here
Other name(s): UDP-galacturonic acid decarboxylase; UDPGalUA carboxy lyase; UDP-D-galacturonate carboxy-lyase
Systematic name: UDP-D-galacturonate carboxy-lyase (UDP-L-arabinose-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-79-9
References:
1.  Fan, D.-F. and Feingold, D.S. UDPgalacturonic acid decarboxylase from Ampullariella digitata. Methods Enzymol. 28B (1972) 438–439.
[EC 4.1.1.67 created 1984]
 
 
EC 5.1.3.5     
Accepted name: UDP-arabinose 4-epimerase
Reaction: UDP-L-arabinose = UDP-D-xylose
For diagram of the biosynthesis of UDP-L-arabinose, UDP-galacturonate and UDP-xylose, click here
Other name(s): uridine diphosphoarabinose epimerase; UDP arabinose epimerase; uridine 5′-diphosphate-D-xylose 4-epimerase; UDP-D-xylose 4-epimerase
Systematic name: UDP-L-arabinose 4-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9024-18-4
References:
1.  Feingold, D.S., Neufeld, E.F. and Hassid, W.Z. The 4-epimerization and decarboxylation of uridine diphosphate D-glucuronic acid by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 910–913. [PMID: 13821949]
[EC 5.1.3.5 created 1965]
 
 
EC 5.1.3.6     
Accepted name: UDP-glucuronate 4-epimerase
Reaction: UDP-glucuronate = UDP-D-galacturonate
For diagram of the biosynthesis of UDP-L-arabinose, UDP-galacturonate and UDP-xylose, click here
Other name(s): uridine diphospho-D-galacturonic acid; UDP glucuronic epimerase; uridine diphosphoglucuronic epimerase; UDP-galacturonate 4-epimerase; uridine diphosphoglucuronate epimerase; UDP-D-galacturonic acid 4-epimerase
Systematic name: UDP-glucuronate 4-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9024-17-3
References:
1.  Feingold, D.S., Neufeld, E.F. and Hassid, W.Z. The 4-epimerization and decarboxylation of uridine diphosphate D-glucuronic acid by extracts from Phaseolus aureus seedlings. J. Biol. Chem. 235 (1960) 910–913. [PMID: 13821949]
[EC 5.1.3.6 created 1965]
 
 
EC 5.1.3.12      
Deleted entry: UDP-glucuronate 5-epimerase. The enzyme has never been purified and the activity was later shown not to exist.
[EC 5.1.3.12 created 1972, deleted 2020]
 
 


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