CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Malate dehydrogenase

Enzyme Information

1.1.1.375
L-2-hydroxycarboxylate dehydrogenase (NAD(P)(+)).
based on mapping to UniProt Q60176
A (2S)-2-hydroxycarboxylate + NAD(P)(+) = a 2-oxocarboxylate + NAD(P)H.
-!- The enzyme from the archaeon Methanocaldococcus jannaschii catalyzes the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3- sulfolactate has the same stereochemical configuration as (2S)-2- hydroxycarboxylates). -!- The enzyme can use both NADH and NADPH, although activity is higher with NADPH. -!- The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP(+). -!- The same organism also possesses an NAD(+)-specific enzyme with similar activity, cf. EC 1.1.1.337.

UniProtKB Entries (1)

Q60176
MDH_METJA
Methanocaldococcus jannaschii DSM 2661
L-2-hydroxycarboxylate dehydrogenase (NAD(P)(+))

PDB Structure

PDB 1HYE
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases.
Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G., Suh, S.W.
J.Mol.Biol.