EC 22.214.171.1245 Enzyme
L-2-hydroxycarboxylate dehydrogenase [NAD(P)+];
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+ [RN:
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) . 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+ . The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC
, L-2-hydroxycarboxylate dehydrogenase (NAD+).
EC 126.96.36.1995 created 2014
Graupner M, Xu H, White RH
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
J Bacteriol 182:3688-92 (2000)
Lee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW
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 307:1351-62 (2001)
The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase.
Mol Microbiol 37:1515-20 (2000)
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