1.1.1.337: L-2-hydroxycarboxylate dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about L-2-hydroxycarboxylate dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.337
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1.1.1.337
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lactobacillus
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confusus
-
dehydrogenases
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l-lactate
-
nadh-dependent
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jannaschii
-
sulfite
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2-oxoisocaproate
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cysteate
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desulfonation
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dogfish
-
methanogen
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methanocaldococcus
-
synthesis
- 1.1.1.337
- lactobacillus
- confusus
- dehydrogenases
- l-lactate
-
nadh-dependent
- jannaschii
- sulfite
- 2-oxoisocaproate
- cysteate
-
desulfonation
-
dogfish
-
methanogen
- methanocaldococcus
- synthesis
Reaction
Synonyms
(R)-sulfolactate dehydrogenase, ComC, L-2-hydroxyacid dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), L-2-hydroxyisocaproate dehydrogenase, L-HicDH, L-hydroxyisocaproate dehydrogenase, L-sulfolactate dehydrogenase, MDH I, MJ1425, sulfolactate dehydrogenase
ECTree
1.1.1.337 L-2-hydroxycarboxylate dehydrogenase (NAD+)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
-
r
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
-
-
-
r
2-hydroxyisocaproate + NAD+
2-oxoisocaproate + NADH + H+
the initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
-
r
2-oxoglutarate + NADH + H+
(S)-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxopentanedioic acid + NADH + H+
2-hydroxypentandioic acid + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NADH + H+
(S)-2-hydroxy-4-methylpentanoate + NAD+
-
-
-
r
glyoxylate + NADH + H+
2-hydroxypropanoate + NAD+
-
-
-
?
oxopropandioic acid + NADH + H+
2-hydroxypropanedioic acid + NAD+
-
-
-
?
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
-
r
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
2-oxocaproate is the best substrate for the wild-type enzyme
-
-
r
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
0.2% activity compared to sulfopyruvate
-
-
r
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
0.2% activity compared to sulfopyruvate
-
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
2-oxoisocaproate is the best substrate with the lowest KM-valus of 0.065 mM. Tthe initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
-
-
-
r
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
-
-
-
?
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
Paracoccus pantotrophus NKNCYSA / DSM 12449
-
-
-
-
?
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
-
-
-
r
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
various 2-oxocarboxylic acids are stereospecifically reduced to the corresponding (S)-2-hydroxycarboxylic acids. In the reverse reaction the NAD+-dependent dehydrogenation of L-2-hydroxycarboxylic acids is observed
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
-
?
oxaloacetate + NADH + H+
malate + NAD+
31% activity compared to sulfopyruvate
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
31% activity compared to sulfopyruvate
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
-
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
preferred substrate
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
-
-
-
r
sulfopyruvate + NADH + H+
sulfo-2-hydroxypropanoate + NAD+
preferred substrate
-
-
r
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
-
?
additional information
?
-
enzyme catalyzes the NADH-dependent reduction of oxaloacetate, 2-oxoglutarate, and pyruvate to the corresponding (S)-2-hydroxyacids with pro-S NADH-stereospecificity
-
-
?
additional information
?
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
-
?
additional information
?
-
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
-
?
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
-
?
additional information
?
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
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-
?
additional information
?
-
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
-
-
?
