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

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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
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+
2.4
Tris
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amine as activator in aldehyde oxidation
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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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
42000
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gel filtration
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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