Accepted name: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
Reaction: a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+
Other name(s): MdhII; lactate/malate dehydrogenase
Systematic name: (2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii catalyses 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) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC, L-2-hydroxycarboxylate dehydrogenase (NAD+).
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [PMID: 10850983]
2.  Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G. and Suh, S.W. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 (2001) 1351–1362. [PMID: 11292347]
3.  Madern, D. The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. Mol. Microbiol. 37 (2000) 1515–1520. [PMID: 10998181]
[EC created 2014]

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