The Enzyme Database

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Accepted name: L-2-hydroxycarboxylate dehydrogenase (NAD+)
Reaction: a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): (R)-sulfolactate:NAD+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; L-2-hydroxyacid dehydrogenase (NAD+); ComC
Systematic name: (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3
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.  Graupner, M. and White, R.H. The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochim. Biophys. Acta 1548 (2001) 169–173. [PMID: 11451450]
3.  Graham, D.E. and White, R.H. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19 (2002) 133–147. [PMID: 12013276]
4.  Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A.M. Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151 (2005) 737–747. [PMID: 15758220]
[EC created 2012]

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