Information on EC 1.2.1.23 - 2-oxoaldehyde dehydrogenase (NAD+)

for references in articles please use BRENDA:EC1.2.1.23
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.2.1.23
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RECOMMENDED NAME
GeneOntology No.
2-oxoaldehyde dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2-oxoaldehyde + NAD+ + H2O = a 2-oxo carboxylate + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylglyoxal degradation VII
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Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-oxoaldehyde:NAD+ 2-oxidoreductase
Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+).
CAS REGISTRY NUMBER
COMMENTARY hide
37250-91-2
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50864-47-6
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97162-76-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
show the reaction diagram
2-oxoaldehydes + NAD+ + H2O
2-oxo acids + NADH
show the reaction diagram
3-deoxygluconosone + NAD+ + H2O
3-deoxygluconic acid + NADH + H+
show the reaction diagram
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-
?
aldehydes + NAD+ + H2O
carboxylic acids + NADH
show the reaction diagram
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-D-glucose + NAD+ + H2O
2-dehydro-3-deoxy-D-gluconate + NADH + H+
show the reaction diagram
3-deoxygluconosone + NAD+ + H2O
3-deoxygluconic acid + NADH + H+
show the reaction diagram
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?
methylglyoxal + NAD+ + H2O
pyruvate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
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3-acetyl-pyridine adenine dinucleotide and thionicotinamide adenine dinucleotide are also effective oxidants
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activation, 66 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-cyclic AMP
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weak inhibition
5,5'-dithiobis(2-nitrobenzoate)
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AMP
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weak inhibition
ATP
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strong inhibitor, 0.6 mM
Barbiturates
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Co2+
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30-40% inhibition at 1.0 mM
Cu2+
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30-40% inhibition at 1.0 mM
cyanide
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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
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GTP
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strong inhibitor, 1 mM
Hg2+
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almost complete inhibition at 1 mM HgCl2
hydrazine
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1-3 mM
hydroxylamine
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1-3 mM
Mn2+
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30-40% inhibition at 1.0 mM
N-ethylmaleimide
N-tris(hydroxymethyl)methylglycine
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NADP+
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-chloromercuribenzoate
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
Semicarbazide
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1-3 mM
Sodium bisulfite
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1 mM
Tris(hydroxymethyl)nitromethane
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50% inhibition at a concentration of 139 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-2-methylpropan-1,3-diol
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activation of aldehyde oxidation
2-amino-2-methylpropan-1-ol
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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
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
glutathione
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activation
Glycerate 3-phosphate
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slightly activation
L-2-Aminopropan-1-ol
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activation of aldehyde oxidation
L-cysteine
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activation
phosphate
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activation
Tris
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activation of aldehyde oxidation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
2-amino-2-methylpropan-1,3-diol
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amine as activator in aldehyde oxidation
15
2-amino-2-methylpropan-1-ol
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amine as activator in aldehyde oxidation
20
2-Aminobutan-1-ol
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amine as activator in aldehyde oxidation
16.6
2-aminopropane
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amine as activator in aldehyde oxidation
7.7
2-aminopropane-1,3-diol
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amine as activator in aldehyde oxidation
1.2
2-keto-3-deoxyglucose
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0.47
3-deoxygluconosone
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5 - 36
L-2-Aminopropan-1-ol
0.24 - 7.14
methylglyoxal
0.03 - 0.5
NAD+
0.0385
pyruvate
pH and temperature not specified in the publication
2.4
Tris
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amine as activator in aldehyde oxidation
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.17
methylglyoxal
pH and temperature not specified in the publication
170
pyruvate
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.73
methylglyoxal
pH and temperature not specified in the publication
4415.6
pyruvate
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.109
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after growth on succinate
0.1334
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0.14
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after growth on threonine
0.571
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1.2
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in crude cell-free extract after growth on threonine
4.65
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8.27
purified native enzyme, pH and temperature not specified in the publication
18.4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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not active below
7.8
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not active below
9.4
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activity increases up to, Tris buffer
10.5
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activity increases up to, carbonate buffer
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
500000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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4 * ?, codominant expression is observed in heterozygotes providing evidence for this enzyme structure
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C, 10 mM potassium phosphate buffer, pH 8.0, 3 weeks
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4°C, pH 7.4, 50 mM NaCl, 5 mM 2-amino-2-methylpropan-1,3-diol, 20 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using acetone powder extract, ammonium sulfate fractionation, alumina C-gamma gel and column chromatography on Sephadex G-200
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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
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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
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using treatment with acetone, ammonium sulfate fractionation, and gel filtration on Sephadex G-25
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
detection of two Mgd loci, which show a restrictive tissue expression, Mgd1 and Mgd2 are preferentially expressed in liver and kidney
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gene ADH1, sequence comparisons
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is highly induced in glutathione GSH-deficient cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information