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The enzyme appears in viruses and cellular organisms
Synonyms 2-ketoaldehyde dehydrogenase, alpha-ketoaldehyde dehydrogenase, methylglyoxal dehydrogenase, NADP-dependent alpha-ketoaldehyde dehydrogenase, NADP-linked alpha-ketoaldehyde dehydrogenase, more
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2-ketoaldehyde dehydrogenase
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alpha-ketoaldehyde dehydrogenase
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methylglyoxal dehydrogenase
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NADP-dependent alpha-ketoaldehyde dehydrogenase
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NADP-linked alpha-ketoaldehyde dehydrogenase
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a 2-oxoaldehyde + NADP+ + H2O = a 2-oxo carboxylate + NADPH + H+
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MetaCyc
methylglyoxal degradation II
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2-oxoaldehyde:NADP+ 2-oxidoreductase
Not identical with EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD+).
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconate + NADPH + H+
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Substrates: - Products: -
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
2-oxoaldehydes + NADP+ + H2O
2-oxo acids + NADPH
methylglyoxal + NADP+ + H2O
pyruvate + NADPH
methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
additional information
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
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Substrates: - Products: -
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
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Substrates: - Products: -
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2-oxoaldehydes + NADP+ + H2O
2-oxo acids + NADPH
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Substrates: - Products: -
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2-oxoaldehydes + NADP+ + H2O
2-oxo acids + NADPH
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Substrates: enzyme from sheep or rat liver also active with NAD+, see also EC 1.2.1.23 Products: -
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2-oxoaldehydes + NADP+ + H2O
2-oxo acids + NADPH
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Substrates: - Products: -
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2-oxoaldehydes + NADP+ + H2O
2-oxo acids + NADPH
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Substrates: enzyme from sheep or rat liver also active with NAD+, see also EC 1.2.1.23 Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH
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Substrates: contributes to the detoxification of methylglyoxal Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: ir Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: ir Products: -
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additional information
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Substrates: the presence of L-2-aminopropan-1-ol is necessary to activate the enzyme Products: -
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additional information
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Substrates: the presence of L-2-aminopropan-1-ol is necessary to activate the enzyme Products: -
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additional information
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Substrates: the presence of amines like Tris, 2-amino-2-methylpropane-1,3-diol, 2-amino-2-methylpropan-1-ol, 2-aminopropane-1,3-diol, 2-aminopropane or 2-aminobutan-1-ol is necessary to activate the enzyme Products: -
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additional information
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Substrates: L-serine methyl ester or L-2-aminopropan-1-ol are necessary to activate the enzyme Products: -
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additional information
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Substrates: the only known amine which activates the enzyme at physiological pH is L-serine methyl ester, L-2-amino-1-propanol gives very little activity but D,L-2-amino-1-propanol activates the enzyme Products: -
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
methylglyoxal + NADP+ + H2O
pyruvate + NADPH
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Substrates: contributes to the detoxification of methylglyoxal Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
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Substrates: - Products: -
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2-keto-3-deoxy-D-glucose + NADP+ + H2O
2-keto-3-deoxy-D-gluconic acid + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: ir Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: - Products: -
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methylglyoxal + NADP+ + H2O
pyruvate + NADPH + H+
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Substrates: ir Products: -
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additional information
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3-acetyl-pyridine adenine dinucleotide and thionicotinamide adenine dinucleotide are also effective oxidants
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NAD+
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Mgd1 and Mgd2 enzymes use also NAD+ as cofactor, see also EC 1.2.1.23
NAD+
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enzyme from sheep or rat liver, see also EC 1.2.1.23
NAD+
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enzyme from sheep or rat liver, see also EC 1.2.1.23
NADP+
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NADP+
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isoenzyme Mgd3 is exclusively NADP+-dependent
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glycine buffer
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complete blockage of the reaction
N-ethylmaleimide
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1-3 mM
N-tris(hydroxymethyl)methylglycine
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p-hydroxymercuribenzoate
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1-3 mM
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2-amino-2-methylpropan-1-ol
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activation of aldehyde oxidation
2-amino-2-methylpropane-1,3-diol
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activation of aldehyde oxidation
2-Aminobutan-1-ol
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activation of aldehyde oxidation
2-aminopropane
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activation of aldehyde oxidation
2-aminopropane-1,3-diol
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activation of aldehyde oxidation
Amines
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several amines stimulate activity
D,L-2-amino-1-propanol
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activation of aldehyde oxidation
DL-2-amino-1-propanol
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required, best activator of the reaction
L-serine methyl ester
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activation of aldehyde oxidation
Tris
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activation of aldehyde oxidation
L-2-Aminopropan-1-ol
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activation of aldehyde oxidation
L-2-Aminopropan-1-ol
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activation of aldehyde oxidation
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1.2
2-keto-3-deoxy-D-glucose
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0.14
methylglyoxal
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0.21 - 0.83
methylglyoxal
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0.21 - 0.83
methylglyoxal
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0.21 - 0.83
methylglyoxal
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0.83
methylglyoxal
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amine as activator in aldehyde oxidation
0.83
methylglyoxal
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in the presence of L-2-aminopropan-1-ol (Km 83 mM), at pH 9.3 and 25°C
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methylglyoxal
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amine as activator in aldehyde oxidation
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methylglyoxal
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in the presence of L-serine methyl ester (Km 8.0 mM)
0.0045
NADP+
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additional information
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10.5
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activity increases up to, carbonate buffer
8.5 - 10
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very low activity at physiological pH
9.3
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activity falls abruptly above
9.4
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activity increases up to, Tris buffer
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inbred strains, recombinant inbred strains
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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43000
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1 * 43000, SDS-PAGE
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monomer
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1 * 43000, SDS-PAGE
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9.3
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not stable above
288259
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4°C, pH 7.4, 50 mM NaCl, 5 mM 2-amino-2-methylpropane-1,3-diol, 20 days
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using acetone powder extract, ammonium sulfate fractionation, alumina C-gamma gel and column chromatography on Sephadex G-200
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using ammonium sulfate fractionation and chromatography on DEAE-Sephadex A-50 column, Blue-dextran affinity column and CM-Sephadex C-50 column
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using ammonium sulfate fractionation and chromatography on DEAE-Sephadex column, Blue-dextran affinity column and CM-Sephadex column
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using ammonium sulfate fractionation, column chromatography on DEAE-cellulose, phosphocellulose, Sephadex G-200, hydroxylapatite, and DEAE-cellulose
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using treatment with acetone, ammonium sulfate fractionation, and gel filtration on Sephadex G-25
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detection of three Mgd loci, which show a restrictive tissue expression, Mgd1 and Mgd2 are preferentially expressed in liver and kidney, Mgd3 is expressed apparently exclusively in heart
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Ray, S.; Ray, M.
Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate
J. Biol. Chem.
257
10566-10570
1982
Capra hircus
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Ray, M.; Ray, S.
On the interaction of nucleotides and glycolytic intermediates with NAD-linked alpha-ketoaldehyde dehydrogenase
J. Biol. Chem.
257
10571-10574
1982
Capra hircus
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Dunkerton, J.; James, S.P.
Some observations on the NADP+-linked oxidation of methylglyoxal catalysed by 2-Oxoaldehyde dehydrogenase
Biochem. J.
153
503-504
1976
Ovis aries
brenda
Dunkerton, J.; James, S.P.
Purification of 2-oxoaldehyde dehydrogenase and its dependence on unusual amines
Biochem. J.
149
609-617
1975
Ovis aries
brenda
Jellum, E.
Metabolism of the ketoaldehyde 2-keto-3-deoxyglucose
Biochim. Biophys. Acta
165
357-363
1968
Ovis aries, Rattus norvegicus
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Monder, C.
alpha-Keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate
J. Biol. Chem.
242
4603-4609
1967
Ovis aries
brenda
Bender, K.; Seibert, R.T.; Wienker, T.F.; Kren, V.; Pravenec, M.; Bissbort, S.
Biochemical genetics of methylglyoxal dehydrogenases in the laboratory rat (Rattus norvegicus)
Biochem. Genet.
32
147-154
1994
Rattus norvegicus
brenda
Vander Jagt, D.L.
2-Ketoaldehyde dehydrogenase from rat liver
Methods Enzymol.
89
513-515
1982
Rattus norvegicus
brenda
Vander Jagt, D.L.; Davidson, L.M.
Purification and characterization of 2-oxoaldehyde dehydrogenase from rat liver
Biochim. Biophys. Acta
484
260-267
1977
Rattus norvegicus
brenda
Vander Jagt, D.L.; Hunsaker, L.A.
Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase
Chem. Biol. Interact.
143-144
341-351
2003
Homo sapiens
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