Continued from EC 5.1.1.1 to EC 5.1.2.6
EC 5.1.3 Acting on Carbohydrates and Derivatives
EC 5.1.99 Acting on Other Compounds
Accepted name: ribulose-phosphate 3-epimerase
Reaction: D-ribulose 5-phosphate = D-xylulose 5-phosphate
For diagram of reaction click here, alternative click here.
Other name(s): phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase
Systematic name: D-ribulose-5-phosphate 3-epimerase
Comments: The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9024-20-8
References:
1. Ashwell, G. and Hickman, J. Enzymatic formation of xylulose 5-phosphate from ribose 5-phosphate in spleen. J. Biol. Chem. 226 (1957) 65-76.
2. Dickens, F. and Williamson, D.H. Pentose phosphate isomerase and epimerase from animal tissues. Biochem. J. 64 (1956) 567-578.
3. Hurwitz, J. and Horecker, B.L. The purification of phosphoketopentoepimerase from Lactobacillus pentosus and the preparation of xylulose 5-phosphate. J. Biol. Chem. 223 (1956) 993-1008.
4. Stumpf, P.K. and Horecker, B.L. The rôle of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus. J. Biol. Chem. 218 (1956) 753-768.
5. Terada, H., Mukae, K., Hosomi, S., Mizoguchi, T. and Uehara, K. Characterization of an enzyme which catalyzes isomerization and epimerization of D-erythrose 4-phosphate. Eur. J. Biochem. 148 (1985) 345-351. [PMID: 3987693]
Accepted name: UDP-glucose 4-epimerase
Reaction: UDP-glucose = UDP-galactose
For diagram of reaction click here.
Other name(s): UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase
Systematic name: UDP-glucose 4-epimerase
Comments: Requires NAD+. Also acts on UDP-2-deoxyglucose.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-89-7
References:
1. Leloir, L.F. Enzymic isomerization and related processes. Adv. Enzymol. Relat. Subj. Biochem. 14 (1953) 193-218.
2. Maxwell, E.S. and de Robichon-Szulmajster, H. Purification of uridine diphosphate galactose-4-epimerase from yeast and the identification of protein-bound diphosphopyridine nucleotide. J. Biol. Chem. 235 (1960) 308-312.
3. Wilson, D.B. and Hogness, D.S. The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase. J. Biol. Chem. 239 (1964) 2469-2481.
Accepted name: aldose 1-epimerase
Reaction: α-D-glucose = β-D-glucose
Other name(s): mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase
Systematic name: aldose 1-epimerase
Comments: Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting β-D-glucose into α-D-glucose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-76-9
References:
1. Bentley, R. and Bhate, D.S. Mutarotase from Penicillium notatum. I. Purification, assay, and general properties of the enzyme. J. Biol. Chem. 235 (1960) 1219-1224. [PMID: 13799037]
2. Bentley, R. and Bhate, D.S. Mutarotase from Penicillium notatum. II. The mechanism of the mutarotation reaction. J. Biol. Chem. 235 (1960) 1225-1233. [PMID: 13799038]
3. Keilin, D. and Hartree, E.F. Biological catalysis of mutarotation of glucose. Biochem. J. 50 (1952) 341-348. [PMID: 14915955]
4. Levy, G.B. and Cook, E.S. A rotographic study of mutarotase. Biochem. J. 57 (1954) 50-55. [PMID: 13159947]
5. Beebe, J.A. and Frey, P.A. Galactose mutarotase: purification, characterization, and investigations of two important histidine residues. Biochemistry 37 (1998) 14989-14997. [PMID: 9778377]
6. Thoden, J.B., Timson, D.J., Reece, R.J. and Holden, H.M. Molecular structure of human galactose mutarotase. J. Biol. Chem. 279 (2004) 23431-23437. [PMID: 15026423]
Accepted name: L-ribulose-5-phosphate 4-epimerase
Reaction: L-ribulose 5-phosphate = D-xylulose 5-phosphate
For diagram click here.
Other name(s): phosphoribulose isomerase; ribulose phosphate 4-epimerase; L-ribulose-phosphate 4-epimerase; L-ribulose 5-phosphate 4-epimerase; AraD; L-Ru5P
Systematic name: L-ribulose-5-phosphate 4-epimerase
Comments: Requires a divalent cation for activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9024-19-5
References:
1. Burma, D.P. and Horecker, B.L. IV.
2. Deupree, J.D. and Wood, W.A. L-Ribulose 5-phosphate 4-epimerase of Aerobacter aerogenes. Evidence for nicotinamide adenine dinucleotide-independent 4-epimerization by the crystalline enzyme. J. Biol. Chem. 245 (1970) 3988-3995. [PMID: 4395381]
3. Lee, N., Patrick, J.W. and Masson, M. Crystalline L-ribulose 5-phosphate 4-epimerase from Escherichia coli. J. Biol. Chem. 243 (1968) 4700-4705. [PMID: 4879898]
4. Wolin, M.J., Simpson, F.J. and Wood, W.A. Degradation of L-arabinose by Aerobacter aerogenes. III. Identification and properties of L-ribulose-5-phosphate 4-epimerase. J. Biol. Chem. 232 (1958) 559-575. [PMID: 13549442]
5. Andersson, A., Schneider, G. and Lindqvist, Y. Purification and preliminary X-ray crystallographic studies of recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia coli. Protein Sci. 4 (1995) 1648-1650. [PMID: 8520491]
6. Lee, L.V., Poyner, R.R., Vu, M.V. and Cleland, W.W. Role of metal ions in the reaction catalyzed by L-ribulose-5-phosphate 4-epimerase. Biochemistry 39 (2000) 4821-4830. [PMID: 10769139]
7. Samuel, J., Luo, Y., Morgan, P.M., Strynadka, N.C. and Tanner, M.E. Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase. Biochemistry 40 (2001) 14772-14780. [PMID: 11732896]
Accepted name: UDP-arabinose 4-epimerase
Reaction: UDP-L-arabinose = UDP-D-xylose
For diagram of reaction 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.
Accepted name: UDP-glucuronate 4-epimerase
Reaction: UDP-glucuronate = UDP-D-galacturonate
For diagram of reaction 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.
Accepted name: UDP-N-acetylglucosamine 4-epimerase
Reaction: UDP-N-acetyl-α-D-glucosamine = UDP-N-acetyl-α-D-galactosamine
For diagram of reaction click here.
Other name(s): UDP acetylglucosamine epimerase; uridine diphosphoacetylglucosamine epimerase; uridine diphosphate N-acetylglucosamine-4-epimerase; uridine 5'-diphospho-N-acetylglucosamine-4-epimerase; UDP-N-acetyl-D-glucosamine 4-epimerase
Systematic name: UDP-N-acetyl-α-D-glucosamine 4-epimerase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-16-2
References:
1. Glaser, L. The biosynthesis of N-acetylgalactosamine. J. Biol. Chem. 234 (1959) 2801-2805.
2. Kornfeld, S. and Glaser, L. The synthesis of thymidine-linked sugars. V. Thymidine diphosphate-amino sugars. J. Biol. Chem. 237 (1962) 3052-3059.
Accepted name: N-acylglucosamine 2-epimerase
Reaction: N-acyl-D-glucosamine = N-acyl-D-mannosamine
Other name(s): acylglucosamine 2-epimerase; N-acetylglucosamine 2-epimerase
Systematic name: N-acyl-D-glucosamine 2-epimerase
Comments: Requires catalytic amounts of ATP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37318-34-6
References:
1. Ghosh, S. and Roseman, S. The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase. J. Biol. Chem. 240 (1965) 1531-1536.
Accepted name: N-acylglucosamine-6-phosphate 2-epimerase
Reaction: N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate
Other name(s): acylglucosamine-6-phosphate 2-epimerase; acylglucosamine phosphate 2-epimerase
Systematic name: N-acyl-D-glucosamine-6-phosphate 2-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37318-35-7
References:
1. Ghosh, S. and Roseman, S. The sialic acids. IV. N-Acyl-D-glucosamine 6-phosphate 2-epimerase. J. Biol. Chem. 240 (1965) 1525-1530. [PMID: 14285487]
Accepted name: CDP-paratose 2-epimerase
Reaction: CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose
For diagram click here.
Other name(s): CDP-paratose epimerase; cytidine diphosphoabequose epimerase; cytidine diphosphodideoxyglucose epimerase; cytidine diphosphoparatose epimerase; cytidine diphosphate paratose-2-epimerase; CDP-abequose epimerase (incorrect); CDP-D-abequose 2-epimerase (incorrect)
Systematic name: CDP-3,6-dideoxy-D-glucose 2-epimerase
Comments: Requires NAD+. CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more systematically called CDP-α-3,6-dideoxy-D-ribo-hexose. CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called CDP-3,6-dideoxy-D-arabino-hexose.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37318-36-8
References:
1. Matsuhashi, S. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. II. Reversible 2-epimerization of cytidine diphosphate paratose. J. Biol. Chem. 241 (1966) 4275-4282. [PMID: 5924649]
2. Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223-256. [PMID: 7826006]
Accepted name: cellobiose epimerase
Reaction: cellobiose = D-glucosyl-D-mannose
Systematic name: cellobiose 2-epimerase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-37-9
References:
1. Tyler, T.R. and Leatherwood, J.M. Epimerization of disaccharides by enzyme preparations from Ruminococcus albus. Arch. Biochem. Biophys. 119 (1967) 363-367. [PMID: 6069974]
Accepted name: UDP-glucuronate 5'-epimerase
Reaction: UDP-glucuronate = UDP-L-iduronate
For diagram of reaction click here.
Other name(s): uridine diphosphoglucuronate 5'-epimerase; UDP-glucuronic acid 5'-epimerase; C-5-uronosyl epimerase
Systematic name: UDP-glucuronate 5'-epimerase
Comments: Requires NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-38-0
References:
1. Jacobson, B. and Davidson, E.A. Biosynthesis of uronic acids by skin enzymes. I. Uridine diphosphate-D-glucuronic acid-5-epimerase. J. Biol. Chem. 237 (1962) 638-642.
Accepted name: dTDP-4-dehydrorhamnose 3,5-epimerase
Reaction: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-4-dehydro-6-deoxy-β-L-mannose
For diagram click here.
Glossary: dTDP-4-dehydro-6-deoxy-β-L-mannose = dTDP-4-dehydro-β-L-rhamnose
Other name(s): dTDP-L-rhamnose synthetase; dTDP-L-rhamnose synthetase; thymidine diphospho-4-ketorhamnose 3,5-epimerase; TDP-4-ketorhamnose 3,5-epimerase; dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase; TDP-4-keto-L-rhamnose-3,5-epimerase; dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase
Systematic name: dTDP-4-dehydro-6-deoxy-α-D-glucose 3,5-epimerase
Comments: The enzyme occurs in a complex with EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37318-39-1
References:
1. Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041-6049. [PMID: 4199258]
2. Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475-1478. [PMID: 4384782]
Accepted name: UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)
Reaction: UDP-N-acetyl-α-D-glucosamine = UDP-N-acetyl-α-D-mannosamine
For diagram of reaction click here
Other name(s): UDP-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphoacetylglucosamine 2'-epimerase (ambiguous); uridine diphospho-N-acetylglucosamine 2'-epimerase (ambiguous); uridine diphosphate-N-acetylglucosamine-2'-epimerase (ambiguous); rffE (gene name); mnaA (gene name); UDP-N-acetyl-D-glucosamine 2-epimerase
Systematic name: UDP-N-acetyl-α-D-glucosamine 2-epimerase
Comments: This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-71-2
References:
1. Kawamura, T., Kimura, M., Yamamori, S. and Ito, E. Enzymatic formation of uridine diphosphate N-acetyl-D-mannosamine. J. Biol. Chem. 253 (1978) 3595-3601. [PMID: 418068]
2. Meier-Dieter, U., Starman, R., Barr, K., Mayer, H. and Rick, P.D. Biosynthesis of enterobacterial common antigen in Escherichia coli. Biochemical characterization of Tn10 insertion mutants defective in enterobacterial common antigen synthesis. J. Biol. Chem. 265 (1990) 13490-13497. [PMID: 2166030]
3. Morgan, P. M., Sala, R. F., and Tanner, M. E. Eliminations in the reactions catalyzed by UDP-N-acetylglucosamine 2-epimerase. J. Am. Chem. Soc. 119 (1997) 10269-10277.
4. Campbell, R.E., Mosimann, S.C., Tanner, M.E. and Strynadka, N.C. The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases. Biochemistry 39 (2000) 14993-15001. [PMID: 11106477]
5. Samuel, J. and Tanner, M.E. Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli. Biochim. Biophys. Acta 1700 (2004) 85-91. [PMID: 15210128]
6. Soldo, B., Lazarevic, V., Pooley, H.M. and Karamata, D. Characterization of a Bacillus subtilis thermosensitive teichoic acid-deficient mutant: gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-epimerase. J. Bacteriol. 184 (2002) 4316-4320. [PMID: 12107153]
Accepted name: glucose-6-phosphate 1-epimerase
Reaction: α-D-glucose 6-phosphate = β-D-glucose 6-phosphate
Systematic name: D-glucose-6-phosphate 1-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37259-65-7
References:
1. Wurster, B. and Hess, B. Glucose-6-phosphate-1-epimerase from baker's yeast. A new enzyme. FEBS Lett. 23 (1972) 341-348.
Accepted name: UDP-glucosamine 4-epimerase
Reaction: UDP-glucosamine = UDP-galactosamine
Systematic name: UDP-glucosamine 4-epimerase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Maley, F. and Maley, G.F. The enzymic conversion of glucosamine to galactosamine. Biochim. Biophys. Acta 31 (1959) 577-578.
2. Silbert, J.E. and Brown, D.H. Enzymic synthesis of uridine diphosphate glucosamine and heparin from [14C]glucosamine by a mouse mast-cell tumor. Biochim. Biophys. Acta 54 (1961) 590-592.
Accepted name: heparosan-N-sulfate-glucuronate 5-epimerase
Reaction: heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate
Other name(s): heparosan epimerase; heparosan-N-sulfate-D-glucuronosyl 5-epimerase; C-5 uronosyl epimerase; polyglucuronate epimerase; D-glucuronyl C-5 epimerase; poly[(1,4)-β-D-glucuronosyl-(1,4)-N-sulfo-α-D-glucosaminyl] glucurono-5-epimerase
Systematic name: poly[(1→4)-β-D-glucuronosyl-(1→4)-N-sulfo-α-D-glucosaminyl] glucurono-5-epimerase
Comments: Acts on D-glucuronosyl residues adjacent to sulfated D-glucosamine units in the heparin precursor. Not identical with EC 5.1.3.19 chondroitin-glucuronate 5-epimerase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112567-86-9
References:
1. Jacobsson, I., Bäckström, G., Höök, M., Lindahl, U., Feingold, D.S., Malmström, A. and Rodén, L. Biosynthesis of heparin. Assay and properties of the microsomal uronosyl C-5 epimerase. J. Biol. Chem. 254 (1979) 2975-2982. [PMID: 107165]
Accepted name: GDP-mannose 3,5-epimerase
Reaction: GDP-mannose = GDP-L-galactose
Other name(s): GDP-D-mannose:GDP-L-galactose epimerase; guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate L-galactose epimerase
Systematic name: GDP-mannose 3,5-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 72162-82-4
References:
1. Barber, G.A. and Hebda, P.A. GDP-D-mannose: GDP-L-galactose epimerase from Chlorella pyrenoidosa. Methods Enzymol. 83 (1982) 522-525. [PMID: 7098948]
2. Hebda, P.A., Behrman, E.J. and Barber, G.A. The guanosine 5'-diphosphate D-mannose: guanosine 5'-diphosphate L-galactose epimerase of Chlorella pyrenoidosa. Chemical synthesis of guanosine 5'-diphosphate L-galactose and further studies of the enzyme and the reaction it catalyzes. Arch. Biochem. Biophys. 194 (1979) 496-502. [PMID: 443816]
Accepted name: chondroitin-glucuronate 5-epimerase
Reaction: chondroitin D-glucuronate = dermatan L-iduronate
For diagram click here.
Other name(s): polyglucuronate 5-epimerase; dermatan-sulfate 5-epimerase; urunosyl C-5 epimerase; chondroitin D-glucuronosyl 5-epimerase
Systematic name: chondroitin-D-glucuronate 5-epimerase
Comments: Not identical with EC 5.1.3.17 heparosan-N-sulfate-glucuronate 5-epimerase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 70766-66-4
References:
1. Malmström, A. and Åberg, L. Biosynthesis of dermatan sulphate. Assay and properties of the uronosyl C-5 epimerase. Biochem. J. 201 (1982) 489-493. [PMID: 7092807]
Accepted name: ADP-glyceromanno-heptose 6-epimerase
Reaction: ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
Systematic name: ADP-L-glycero-D-manno-heptose 6-epimerase
Comments: requires NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85030-75-7
References:
1. Ding, L., Seto, B.L., Ahmed, S.A., Coleman, W.G., Jr. Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosugar epimerase, ADP-L-glycero-D-manno-heptose 6-epimerase. J. Biol. Chem. 269 (1994) 24384-24390. [PMID: 7929099]
2. Raetz, C.R.H. Biochemistry of endotoxins. Annu. Rev. Biochem. 58 (1990) 129-170. [PMID: 1695830]
Accepted name: maltose epimerase
Reaction: α-maltose = β-maltose
Systematic name: maltose 1-epimerase
Comments: The enzyme catalyses the interconversion of α and β anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 166799-98-0
References:
1. Shirokane, Y. and Suzuki, M. A novel enzyme, maltose 1-epimerase from Lactobacillus brevis IFO 3345. FEBS Lett. 367 (1995) 177-179. [PMID: 7796915]
Accepted name: L-ribulose-5-phosphate 3-epimerase
Reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate
For diagram click here.
Other name(s): L-xylulose 5-phosphate 3-epimerase; UlaE; SgaU
Systematic name: L-ribulose-5-phosphate 3-epimerase
Comments: Along with EC 4.1.1.85, 3-dehydro-L-gulonate-6-phosphate decarboxylase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1114425-98-7
References:
1. Yew, W.S. and Gerlt, J.A. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yif-sga and yia-sgb operons. J. Bacteriol. 184 (2002) 302-306. [PMID: 11741871]
Accepted name: UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase
Reaction: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronate
For diagram of reaction, click here
Glossary: UDP-α-D-GlcNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid
UDP-α-D-ManNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid
Other name(s): UDP-GlcNAc3NAcA 2-epimerase; UDP-α-D-GlcNAc3NAcA 2-epimerase; 2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerase; WbpI; WlbD
Systematic name: 2,3-diacetamido-2,3-dideoxy-α-D-glucuronate 2-epimerase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of the B-band lipopolysaccharide of Pseudomonas aeroginosa serotype O5 and of the band-A trisaccharide of Bordetella pertussis, both important respiratory pathogens [1]. The enzyme is highly specific as UDP-α-D-GlcNAc, UDP-α-D-GlcNAcA (UDP-2-acetamido-2-deoxy-α-D-glucuronic acid) and UDP-α-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucose) cannot act as substrates [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 123-130. [PMID: 17346239]
2. Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Erratum report: Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 625 only.
3. Sri Kannathasan, V., Staines, A.G., Dong, C.J., Field, R.A., Preston, A.G., Maskell, D.J. and Naismith, J.H. Overexpression, purification, crystallization and data collection on the Bordetella pertussis wlbD gene product, a putative UDP-GlcNAc 2′-epimerase. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1310-1312. [PMID: 11526328]
Accepted name: N-acetylneuraminate epimerase
Reaction: N-acetyl-α-neuraminate = N-acetyl-β-neuraminate
Other name(s): sialic acid epimerase; N-acetylneuraminate mutarotase; YjhT
Systematic name: N-acetyl-α-neuraminate 2-epimerase
Comments: Sialoglycoconjugates present in vertebrates are linked exclusively by α-linkages and are released in α form during degradation. This enzyme accelerates maturotation to the β form (which also occurs as a slow spontaneous reaction), which is necessary for further metabolism by the bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, CAS registry number:
References:
1. Severi, E., Müller, A., Potts, J.R., Leech, A., Williamson, D., Wilson, K.S. and Thomas, G.H. Sialic acid mutarotation is catalyzed by the Escherichia coli β-propeller protein YjhT. J. Biol. Chem. 283 (2008) 4841-4849. [PMID: 18063573]
Accepted name: dTDP-L-rhamnose 4-epimerase
Reaction: dTDP-6-deoxy-β-L-talose = dTDP-6-deoxy-β-L-mannose
Glossary: dTDP-6-deoxy-β-L-mannose = dTDP-4-β-L-rhamnose
Other name(s): dTDP-4-L-rhamnose 4-epimerase; wbiB (gene name)
Systematic name: dTDP-6-deoxy-β-L-talose 4-epimerase
Comments: The equilibrium is strongly towards dTDP-6-deoxy-β-L-mannose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Yoo, H.G., Kwon, S.Y., Karki, S. and Kwon, H.J. A new route to dTDP-6-deoxy-L-talose and dTDP-L-rhamnose: dTDP-L-rhamnose 4-epimerase in Burkholderia thailandensis. Bioorg. Med. Chem. Lett. 21 (2011) 3914-3917. [PMID: 21640586]
Accepted name: methylmalonyl-CoA epimerase
Reaction: (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA
Other name(s): methylmalonyl-CoA racemase; methylmalonyl coenzyme A racemase; DL-methylmalonyl-CoA racemase; 2-methyl-3-oxopropanoyl-CoA 2-epimerase [incorrect]
Systematic name: methylmalonyl-CoA 2-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, Metacyc, CAS registry number: 9024-03-7
References:
1. Mazumder, R., Sasakawa, T., Kaziro, Y. and Ochoa, S. Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase. J. Biol. Chem. 237 (1962) 3065-3068.
2. Overath, P., Kellerman, G.M., Lynen, F., Fritz, H.P. and Keller, H.J. Zum Mechanismus der Umlagerung von Methylmalonyl-CoA in Succinyl-CoA. II. Versuche zur Wirkungsweise von Methylmalonyl-CoA-Isomerase and Methylmalonyl-CoA-Racemase. Biochem. Z. 335 (1962) 500-518.
Accepted name: 16-hydroxysteroid epimerase
Reaction: 16α-hydroxysteroid = 16β-hydroxysteroid
Systematic name: 16-hydroxysteroid 16-epimerase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37318-40-4
References:
1. Dahm, K., Lindlau, M. and Breuer, H. Steroid epimerase-a new enzyme of estrogen metabolism. Biochim. Biophys. Acta 159 (1968) 377-389. [PMID: 5657462]
Accepted name: allantoin racemase
Reaction: (S)(+)-allantoin = (R)(–)-allantoin
For diagram click here.
Systematic name: allantoin racemase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56214-40-5
References:
1. van der Drift, L., Vogels, G.D. and van der Drift, C. Allantoin racemase: a new enzyme from Pseudomonas species. Biochim. Biophys. Acta 391 (1975) 240-248. [PMID: 237557]
Accepted name: α-methylacyl-CoA racemase
Reaction: (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA
For diagram click here.
Systematic name: 2-methylacyl-CoA 2-epimerase
Comments: α-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 156681-44-6
References:
1. Schmitz, W., Fingerhut, R., Conzelmann, E. Purification and properties of an α-methylacyl-CoA racemase from rat liver. Eur. J. Biochem. 222 (1994) 313-323. [PMID: 8020470]
Accepted name: hydantoin racemase
Reaction: D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin
Glossary: hydantoin = imidazolidine-2,4-dione
Other name(s): 5'-monosubstituted-hydantoin racemase; HyuA; HyuE
Systematic name: D-5-monosubstituted-hydantoin racemase
Comments: This enzyme, along with N-carbamoylase (EC 3.5.1.77 and EC 3.5.1.87) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [7]. The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-(2-methylthioethyl)hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position [2]. In the enzyme from Sinorhizobium meliloti, Cys76 is responsible for recognition and proton retrieval of D-isomers, while Cys181 is responsible for L-isomer recognition and racemization [6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Watabe, K., Ishikawa, T., Mukohara, Y. and Nakamura, H. Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli. J. Bacteriol. 174 (1992) 7989-7995. [PMID: 1459947]
2. Wiese, A., Pietzsch, M., Syldatk, C., Mattes, R. and Altenbuchner, J. Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization. J. Biotechnol. 80 (2000) 217-230. [PMID: 10949312]
3. Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Mingorance-Cazorla, L., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114. Appl. Environ. Microbiol. 70 (2004) 625-630. [PMID: 14711700]
4. Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58. Biochimie 86 (2004) 77-81. [PMID: 15016445]
5. Suzuki, S., Onishi, N. and Yokozeki, K. Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912. Biosci. Biotechnol. Biochem. 69 (2005) 530-536. [PMID: 15784981]
6. Martínez-Rodríguez, S., Andújar-Sánchez, M., Neira, J.L., Clemente-Jiménez, J.M., Jara-Pérez, V., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti. Protein Sci. 15 (2006) 2729-2738. [PMID: 17132860]
7. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]
Accepted name: NAD(P)H-hydrate epimerase
Reaction: (1) (6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
(2) (6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
Glossary: 6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = NADHX = NADH-hydrate
6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = NADPHX = NADPH-hydrate
Other name(s): NAD(P)HX epimerase
Systematic name: (6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide 6-epimerase
Comments: The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Marbaix, A.Y., Noel, G., Detroux, A.M., Vertommen, D., Van Schaftingen, E. and Linster, C.L. Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J. Biol. Chem. 286 (2011) 41246-41252. [PMID: 21994945]