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EC Tree
IUBMB Comments Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
methylglyoxal dehydrogenase, 2-ketoaldehyde dehydrogenase,
more
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2-ketoaldehyde dehydrogenase
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alpha-ketoaldehyde dehydrogenase
methylglyoxal dehydrogenase
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-
-
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NAD+-linked alcohol dehydrogenase 1
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NAD+-linked methylglyoxal dehydrogenase
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NAD-dependent alpha-ketoaldehyde dehydrogenase
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-
-
-
NAD-linked alpha-ketoaldehyde dehydrogenase
-
-
-
-
alpha-ketoaldehyde dehydrogenase
-
-
-
-
alpha-ketoaldehyde dehydrogenase
-
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a 2-oxoaldehyde + NAD+ + H2O = a 2-oxo carboxylate + NADH + H+
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-
-
-
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2-oxoaldehyde:NAD+ 2-oxidoreductase
Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).
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2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
3-deoxygluconosone + NAD+ + H2O
3-deoxygluconic acid + NADH + H+
-
-
-
?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
additional information
?
-
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
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-
levels in diabetic patients are significantly higher compared with healthy subjects in both erythrocytes and plasma
?
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
-
-
-
?
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
-
-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
-
-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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enzyme from sheep or rat liver also active with NADP+, see also EC 1.2.1.49
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?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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enzyme from sheep or rat liver also active with NADP+, see also EC 1.2.1.49
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?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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enzyme from sheep or rat liver also active with NADP+, see also EC 1.2.1.49
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?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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enzyme from sheep or rat liver also active with NADP+, see also EC 1.2.1.49
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?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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-
-
?
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
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enzyme from sheep or rat liver also active with NADP+, see also EC 1.2.1.49
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?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
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-
-
?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
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-
-
?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
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-
-
?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
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-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
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i.e. pyruvaldehyde
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?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
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-
-
r
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
the reduction reaction is highly preferred
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r
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
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ir
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
additional information
?
-
Candida albicans ADH1 is a bifunctional enzyme that catalyzes methylglyoxal oxidation and reduction, cf. EC 1.1.1.1
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-
?
additional information
?
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Candida albicans ADH1 is a bifunctional enzyme that catalyzes methylglyoxal oxidation and reduction, cf. EC 1.1.1.1
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-
?
additional information
?
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the presence of L-2-aminopropan-1-ol is necessary to activate the enzyme
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-
?
additional information
?
-
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the presence of L-2-aminopropan-1-ol is necessary to activate the enzyme
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?
additional information
?
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the presence of amines like Tris, 2-amino-2-methylpropan-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
-
-
?
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2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
3-deoxygluconosone + NAD+ + H2O
3-deoxygluconic acid + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
-
-
levels in diabetic patients are significantly higher compared with healthy subjects in both erythrocytes and plasma
?
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
-
-
-
?
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
-
r
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
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?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
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ir
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
-
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
-
i.e. pyruvaldehyde
-
?
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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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-
NADP+
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can not substitute for NAD
NADP+
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enzyme from sheep or rat liver, see also EC 1.2.1.49
NADP+
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enzyme from sheep or rat liver, see also EC 1.2.1.49
NADP+
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Mgd1 and Mgd2 enzymes use also NADP+ as cofactor, see also EC 1.2.1.49
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Mg2+
-
activation less effective than with Ca2+
Mg2+
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35% activation at 2.5 mM and 50% activation at 5.0 mM MgCl2
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3',5'-cyclic AMP
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weak inhibition
5,5'-dithiobis(2-nitrobenzoate)
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ATP
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strong inhibitor, 0.6 mM
Co2+
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30-40% inhibition at 1.0 mM
Cu2+
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30-40% inhibition at 1.0 mM
diethanolamine
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causes 40% inhibition of the enzyme activated by L-2-aminopropan-1-ol at a concentration of 50 mM
EDTA
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60% inhibition at 5 mM, 87% inhibition at 10 mM
glyceraldehyde 3-phosphate
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strong inhibitor
glycine buffer
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complete blockage of the reaction
GTP
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strong inhibitor, 1 mM
Hg2+
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almost complete inhibition at 1 mM HgCl2
Mn2+
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30-40% inhibition at 1.0 mM
N-tris(hydroxymethyl)methylglycine
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Ni2+
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30-40% inhibition at 1.0 mM
Nitro-alcohols
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analogues of the activating amines, at large concentrations, 66-83 mM
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oxalate
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60% inhibition at 5 mM, 96% inhibition at 10 mM
p-hydroxymercuribenzoate
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1-3 mM
phosphate
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inhibits the enzyme prepared from the acetone-dried liver extract, 10-20 mM
Tris(hydroxymethyl)nitromethane
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50% inhibition at a concentration of 139 mM
ADP
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strong inhibitor, 1 mM
barbiturates
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at large concentrations, 6-46 mM
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N-ethylmaleimide
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1 mM
NADP+
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strong competitive inhibitor, 0.001 mM
NADP+
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50% inhibition at 2.0 mM and 80% at 5.0 mM
p-chloromercuribenzoate
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-
p-chloromercuribenzoate
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-
p-chloromercuribenzoate
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-
p-chloromercuribenzoate
-
0.1 mM
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2-amino-2-methylpropan-1,3-diol
-
activation of aldehyde oxidation
2-amino-2-methylpropan-1-ol
-
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
beta-mercaptoethanol
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restores the activity after inactivation with p-chloromercuribenzoate
dihydroxyacetone phosphate
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stimulation
dithiothreitol
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activation
fructose 1,6-bisphosphate
Glycerate 3-phosphate
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slightly activation
L-2-Aminopropan-1-ol
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activation of aldehyde oxidation
Tris
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activation of aldehyde oxidation
fructose 1,6-bisphosphate
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100% stimulation, 0.03 mM, extent of stimulation is pH-dependent
fructose 1,6-bisphosphate
-
slightly activation
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16.6
2-aminopropane
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amine as activator in aldehyde oxidation
1.2
2-dehydro-3-deoxy-D-glucos
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0.47
3-deoxygluconosone
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0.24 - 7.14
methylglyoxal
0.0385
pyruvate
pH and temperature not specified in the publication
0.24
methylglyoxal
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-
0.97
methylglyoxal
pH and temperature not specified in the publication
2.08
methylglyoxal
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assay mixture containing 40 mM L-2-aminopropan-1-ol and 10 mM potassium phosphate
2.08
methylglyoxal
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amine as activator in aldehyde oxidation, same value for methylglyoxal as substrate, assay mixture containing 10 mM potassium phosphate
2.08
methylglyoxal
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in the presence of L-2-aminopropan-1-ol (Km 5.0 mM) and 10 mM phosphate, at pH 9.3 and 25°C
2.08
methylglyoxal
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in the presence of L-2-aminopropan-1-ol (Km 5.0 mM), at pH 9.3 and 25°C
2.6
methylglyoxal
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amine as activator in aldehyde oxidation
2.6
methylglyoxal
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assay mixture containing 40 mM 2-amino-2-methylpropan-1-ol and 10 mM potassium phosphate
2.6
methylglyoxal
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in the presence of 2-amino-2-methylpropan-1-ol (Km 15 mM), at pH 9.3 and 25°C
3.8
methylglyoxal
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amine as activator in aldehyde oxidation
3.8
methylglyoxal
-
assay mixture containing 40 mM 2-aminobutan-1-ol and 10 mM potassium phosphate
3.8
methylglyoxal
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in the presence of 2-aminobutan-1-ol (Km 20 mM), at pH 9.3 and 25°C
4
methylglyoxal
-
amine as activator in aldehyde oxidation
4
methylglyoxal
-
assay mixture containing 40 mM Tris and 10 mM potassium phosphate
4
methylglyoxal
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in the presence of Tris (Km 2.4 mM), at pH 9.3 and 25°C
5
methylglyoxal
-
amine as activator in aldehyde oxidation
5
methylglyoxal
-
in the presence of 2-amino-2-methylpropan-1,3-diol (Km 4.3 mM), at pH 9.3 and 25°C
5.5
methylglyoxal
-
amine as activator in aldehyde oxidation
5.5
methylglyoxal
-
assay mixture containing 40 mM 2-aminopropane-1,3-diol and 10 mM potassium phosphate
5.5
methylglyoxal
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in the presence of 2-aminopropane-1,3-diol (Km 7.7 mM), at pH 9.3 and 25°C
7.14
methylglyoxal
-
assay mixture containing 40 mM L-2-aminopropan-1-ol, no potassium phosphate
7.14
methylglyoxal
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amine as activator in aldehyde oxidation, assay mixture containing 5 mM methylglyoxal, no potassium phosphate
7.14
methylglyoxal
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in the presence of L-2-aminopropan-1-ol (Km 36 mM), without phosphate, at pH 9.3 and 25°C
0.03
NAD+
-
-
0.11
NAD+
-
assay mixture containing 40 mM L-2-aminopropan-1-ol, 5 mM methylglyoxal and 10 mM potassium phosphate
0.32
NAD+
-
assay mixture containing 40 mM L-2-aminopropan-1-ol, 5 mM methylglyoxal, no potassium phosphate
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18.17
methylglyoxal
pH and temperature not specified in the publication
170
pyruvate
pH and temperature not specified in the publication
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18.73
methylglyoxal
pH and temperature not specified in the publication
4415.6
pyruvate
pH and temperature not specified in the publication
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0.109
-
after growth on succinate
0.14
-
after growth on threonine
1.2
-
in crude cell-free extract after growth on threonine
8.27
purified native enzyme, pH and temperature not specified in the publication
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8
-
-
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10.5
-
activity increases up to, carbonate buffer
9.4
-
activity increases up to, Tris buffer
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
inbred strains, recombinant inbred strains
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
methylglyoxal accumulation leads to G2-phase arrest by affecting cell growth, ROS production, viability, differentiation, and virulence. Phenotypes of enzyme-deficient cells, overview
physiological function
the enzyme catalyzes both methylglyoxal oxidation to pyruvate as well as its reduction to acetol. ADH1 activity likely shifts between methylglyoxal oxidation and reduction with a marked change in the intracellular redox state during the growth, such as GSH starvation. The enzyme is required for regulation of methylglyoxal content in the cell. Mgd activity is highly induced in GSH-deficient cells
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A0A1D8PP43_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
350
0
36909
TrEMBL
Chloroplast (Reliability: 1 )
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42000
-
gel filtration
42000
-
1 * 42000, SDS-PAGE
43000
-
gel filtration
43000
-
1 * 43000, SDS-PAGE
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tetramer
-
4 * ?, codominant expression is observed in heterozygotes providing evidence for this enzyme structure
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
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additional information
generation of ADH1 gene disruption mutants
additional information
-
generation of ADH1 gene disruption mutants
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4°C or -20°C, 10 mM potassium phosphate buffer, pH 8.0, 3 weeks
-
4°C, pH 7.4, 50 mM NaCl, 5 mM 2-amino-2-methylpropan-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
-
using acetone powder extract, ammonium sulfate precipitation, calcium phosphate gel treatment, column chromatography on DEAE-cellulose and NAD-Agarose, separated from the NADP-dependent enzyme through affinity chromatography on a thiol-Sepharose column
-
using acetone powder preparation, ammonium sulfate, column chromatography on DEAE-cellulose, affinity column packed with TSK-Gel AF-Red Toyopearl 650 ML and fast protein liquid chromatography
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using ammonium sulfate fractionation and column chromatography on DEAE-cellulose, phosphocellulose, hydroxyapatite and Sephadex G-200
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using ammonium sulfate fractionation, column chromatography on DEAE-cellulose, Phosphocellulose, Sephadex G-200, Hydroxylapatite, and a second DEAE-cellulose step
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using column chromatography on DEAE-cellulose, Butyl-Toyopearl 650M, Sephadex G-150, hydroxylapatite, Blue-dextran and Sepharose CL-6B
-
using treatment with acetone, ammonium sulfate fractionation, and gel filtration on Sephadex G-25
-
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detection of two Mgd loci, which show a restrictive tissue expression, Mgd1 and Mgd2 are preferentially expressed in liver and kidney
-
gene ADH1, sequence comparisons
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the enzyme activity is highly induced in glutathione GSH-deficient cells
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Oimomi, M.; Hata, F.; Nakamichi, T.; Baba, S.; Kato, H.
Purification of alpha-ketoaldehyde dehydrogenase from the human liver and its possible significance in the control of glycation
Experientia
45
463-466
1989
Homo sapiens
brenda
Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.
Metabolism of 2-ketoaldehydes in bacteria: oxidative conversion of methylglyoxal to pyruvate by an enzyme from Pseudomonas putida
Agric. Biol. Chem.
51
1059-1066
1987
Pseudomonas putida
-
brenda
Saez, G.T.; Blay, P.; Vina, J.R.; Vina, J.
Glucose formation from methylglyoxal in rat hepatocytes
Biochem. Soc. Trans.
13
945-946
1985
Rattus norvegicus
-
brenda
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
brenda
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
brenda
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
Willetts, A.J.; Turner, J.M.
Threonine metabolism in a strain of Bacillus subtilis: enzymes acting on methylglyoxal
Biochim. Biophys. Acta
222
668-670
1970
Bacillus subtilis
brenda
Jellum, E.
Metabolism of the ketoaldehyde 2-keto-3-deoxyglucose
Biochim. Biophys. Acta
165
357-363
1968
Ovis aries, Rattus norvegicus
brenda
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
Fujii, E.; Iwase, H.; Ishii-Karakasa, I.; Yajima, Y.; Hotta, K.
The presence of 2-keto-3-deoxygluconic acid and oxoaldehyde dehydrogenase activity in human erythrocytes
Biochem. Biophys. Res. Commun.
210
852-857
1995
Homo sapiens
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
Kwak, M.K.; Ku, M.; Kang, S.O.
NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans
FEBS Lett.
588
1144-1153
2014
Candida albicans (A0A1D8PP43), Candida albicans
brenda
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