1.1.1.375: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about L-2-hydroxycarboxylate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.375
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1.1.1.375
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dehydrogenases
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methanococcus
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jannaschii
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l-lactate
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nadh-dependent
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hyperthermophilic
- 1.1.1.375
- dehydrogenases
-
methanococcus
- jannaschii
- l-lactate
-
nadh-dependent
-
hyperthermophilic
Reaction
Synonyms
lactate/malate dehydrogenase, LDH-like L-MalDH, MdhII, MJ0409, MJ0490
ECTree
1.1.1.375 L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]Advanced search results
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results (Cofactor
Cofactor on EC 1.1.1.375 - L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
NAD+
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
NAD+
the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate
NADH
preference of NADP(H) over NAD(H).. The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
NADH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
NADH
the enzyme prefers NADPH over NADH in reduction of oxaloacetate
NADP+
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
NADP+
the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate
NADPH
preference of NADP(H) over NAD(H). The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
NADPH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
NADPH
the enzyme prefers NADPH over NADH in reduction of oxaloacetate or 3-sulfopyruvate
