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
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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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Subunits
Subunits on EC 1.1.1.375 - L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme. Enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition at pH 7 without dissociation of the subunits
tetramer
tetramer
the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme
tetramer
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the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme
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