The Enzyme Database

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EC 1.1.1.78     
Accepted name: methylglyoxal reductase (NADH)
Reaction: (R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent)
Systematic name: (R)-lactaldehyde:NAD+ oxidoreductase
Comments: This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-16-1
References:
1.  Ting, S.-M., Miller, O.N. and Sellinger, O.Z. The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver. Biochim. Biophys. Acta 97 (1965) 407–415. [DOI] [PMID: 14323585]
2.  Ray, M. and Ray, S. Purification and partial characterization of a methylglyoxal reductase from goat liver. Biochim. Biophys. Acta 802 (1984) 119–127. [DOI] [PMID: 6386056]
[EC 1.1.1.78 created 1972, modified 2005, modified 2013]
 
 
EC 1.1.1.283     
Accepted name: methylglyoxal reductase (NADPH)
Reaction: (S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase
Systematic name: (S)-lactaldehyde:NADP+ oxidoreductase
Comments: The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78310-66-4
References:
1.  Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T. and Kimura, A. Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur. J. Biochem. 151 (1985) 631–636. [DOI] [PMID: 3896793]
2.  Chen, C.N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L.G., Dover, J.L., Johnston, M., Chitnis, P.R. and Kohl, D.H. Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae. Yeast 20 (2003) 545–554. [DOI] [PMID: 12722185]
3.  Hauser, M., Horn, P., Tournu, H., Hauser, N.C., Hoheisel, J.D., Brown, A.J. and Dickinson, J.R. A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase. FEMS Yeast Res. 7 (2007) 84–92. [DOI] [PMID: 16999827]
4.  Muller, M., Katzberg, M., Bertau, M. and Hummel, W. Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae. Org. Biomol. Chem. 8 (2010) 1540–1550. [DOI] [PMID: 20237665]
5.  Choi, Y.H., Choi, H.J., Kim, D., Uhm, K.N. and Kim, H.K. Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using Saccharomyces cerevisiae reductase with high enantioselectivity. Appl. Microbiol. Biotechnol. 87 (2010) 185–193. [DOI] [PMID: 20111861]
6.  Breicha, K., Muller, M., Hummel, W. and Niefind, K. Crystallization and preliminary crystallographic analysis of Gre2p, an NADP+-dependent alcohol dehydrogenase from Saccharomyces cerevisiae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 838–841. [DOI] [PMID: 20606287]
[EC 1.1.1.283 created 2005, modified 2013]
 
 
EC 1.2.3.15     
Accepted name: (methyl)glyoxal oxidase
Reaction: (1) glyoxal + H2O + O2 = glyoxylate + H2O2
(2) 2-oxopropanal + H2O + O2 = pyruvate + H2O2
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): glx1 (gene name); glx2 (gene name)
Systematic name: (methyl)glyoxal:oxygen oxidoreductase
Comments: The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kersten, P.J. and Kirk, T.K. Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium. J. Bacteriol. 169 (1987) 2195–2201. [DOI] [PMID: 3553159]
2.  Kersten, P.J. and Cullen, D. Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Proc. Natl. Acad. Sci. USA 90 (1993) 7411–7413. [DOI] [PMID: 8346264]
3.  Kersten, P.J., Witek, C., vanden Wymelenberg, A. and Cullen, D. Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic variants: structure, genomic organization, and heterologous expression of glx1 and glx2. J. Bacteriol. 177 (1995) 6106–6110. [DOI] [PMID: 7592374]
4.  Whittaker, M.M., Kersten, P.J., Nakamura, N., Sanders-Loehr, J., Schweizer, E.S. and Whittaker, J.W. Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase. J. Biol. Chem. 271 (1996) 681–687. [DOI] [PMID: 8557673]
[EC 1.2.3.15 created 2016]
 
 
EC 1.13.11.50     
Accepted name: acetylacetone-cleaving enzyme
Reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): Dke1; acetylacetone dioxygenase; diketone cleaving dioxygenase; diketone cleaving enzyme
Systematic name: acetylacetone:oxygen oxidoreductase
Comments: An Fe(II)-dependent enzyme. Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii. While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 524047-53-8
References:
1.  Straganz, G.D., Glieder, A., Brecker, L., Ribbons, D.W. and Steiner, W. Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii. Biochem. J. 369 (2003) 573–581. [DOI] [PMID: 12379146]
[EC 1.13.11.50 created 2003]
 
 
EC 2.2.1.11     
Accepted name: 6-deoxy-5-ketofructose 1-phosphate synthase
Reaction: (1) 2-oxopropanal + D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
(2) 2-oxopropanal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
For diagram of 3-dehydroquinate biosynthesis in archaea, click here
Glossary: 2-oxopropanal = methylglyoxal
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
Other name(s): DKFP synthase
Systematic name: 2-oxopropanal:D-fructose 1,6-bisphosphate glycerone-phosphotransferase
Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  White, R.H. and Xu, H. Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii. Biochemistry 45 (2006) 12366–12379. [DOI] [PMID: 17014089]
2.  Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36–41. [DOI] [PMID: 18318840]
[EC 2.2.1.11 created 2012]
 
 
EC 3.5.1.124     
Accepted name: protein deglycase
Reaction: (1) an Nω-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + lactate
(2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate
(3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + lactate
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): PARK7 (gene name); DJ-1 protein; yhbO (gene name); yajL (gene name); glyoxylase III (incorrect)
Systematic name: a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]
Comments: The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Misra, K., Banerjee, A.B., Ray, S. and Ray, M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem. J. 305 (1995) 999–1003. [PMID: 7848303]
2.  Subedi, K.P., Choi, D., Kim, I., Min, B. and Park, C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol. Microbiol. 81 (2011) 926–936. [DOI] [PMID: 21696459]
3.  Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T. and Lamouri, A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290 (2015) 1885–1897. [DOI] [PMID: 25416785]
4.  Mihoub, M., Abdallah, J., Gontero, B., Dairou, J. and Richarme, G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463 (2015) 1305–1310. [DOI] [PMID: 26102038]
5.  Abdallah, J., Mihoub, M., Gautier, V. and Richarme, G. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 470 (2016) 282–286. [DOI] [PMID: 26774339]
[EC 3.5.1.124 created 2016]
 
 
EC 4.2.1.130     
Accepted name: D-lactate dehydratase
Reaction: (R)-lactate = 2-oxopropanal + H2O
Glossary: methylglyoxal = 2-oxopropanal
(R)-lactate = D-lactate
Other name(s): glyoxylase III; GLO3
Systematic name: (R)-lactate hydro-lyase
Comments: The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hasim, S., Hussin, N.A., Alomar, F., Bidasee, K.R., Nickerson, K.W. and Wilson, M.A. A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans. J. Biol. Chem. 289 (2014) 1662–1674. [DOI] [PMID: 24302734]
2.  Zhao, Q., Su, Y., Wang, Z., Chen, C., Wu, T. and Huang, Y. Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe. BMC Evol Biol 14:86 (2014). [DOI] [PMID: 24758716]
[EC 4.2.1.130 created 2011]
 
 
EC 4.2.3.3     
Accepted name: methylglyoxal synthase
Reaction: glycerone phosphate = 2-oxopropanal + phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
2-oxopropanal = methylglyoxal
Other name(s): methylglyoxal synthetase; glycerone-phosphate phospho-lyase
Systematic name: glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Comments: Does not act on D-glyceraldehyde 3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37279-01-9
References:
1.  Cooper, R.A. and Anderson, A. The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli. FEBS Lett. 11 (1970) 273–276. [DOI] [PMID: 11945504]
2.  Hopper, D.J. and Cooper, R.A. The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis? FEBS Lett. 13 (1971) 213–216. [DOI] [PMID: 11945670]
3.  Ray, S. and Ray, M. Isolation of methylglyoxal synthase from goat liver. J. Biol. Chem. 256 (1981) 6230–6233. [PMID: 7240200]
[EC 4.2.3.3 created 1972 as EC 4.2.99.11, transferred 2000 to EC 4.2.3.3]
 
 
EC 4.4.1.5     
Accepted name: lactoylglutathione lyase
Reaction: (R)-S-lactoylglutathione = glutathione + 2-oxopropanal
Glossary: 2-oxopropanal = methylglyoxal
Other name(s): methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing)
Systematic name: (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing; glutathione-forming)
Comments: Also acts on 3-phosphoglycerol-glutathione.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9033-12-9
References:
1.  Ekwall, K. and Mannervik, B. The stereochemical configuration of the lactoyl group of S-lactoylglutathionine formed by the action of glyoxalase I from porcine erythrocytes and yeast. Biochim. Biophys. Acta 297 (1973) 297–299. [DOI] [PMID: 4574550]
2.  Racker, E. The mechanism of action of glyoxalase. J. Biol. Chem. 190 (1951) 685–696. [PMID: 14841219]
[EC 4.4.1.5 created 1961]
 
 


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