L-2-hydroxycarboxylate dehydrogenase (NAD+)

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L-2-hydroxycarboxylate dehydrogenase (NAD+)
EC number
CAS number 81210-65-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

L-2-hydroxycarboxylate dehydrogenase (NAD+) (EC, (R)-sulfolactate:NAD+ oxidoreductase, L-sulfolactate dehydrogenase, (R)-sulfolactate dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), ComC) is an enzyme with systematic name (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction

(2S)-2-hydroxycarboxylate + NAD+ 2-oxocarboxylate + NADH + H+

The enzyme from the archaeon Methanocaldococcus jannaschii uses as a substrate multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate.


  1. ^ Graupner, M.; Xu, H.; White, R. H. (2000). "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". J. Bacteriol. 182: 3688–3692. doi:10.1128/JB.182.13.3688-3692.2000. PMC 94539Freely accessible. PMID 10850983. 
  2. ^ Graupner, M.; White, R. H. (2001). "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: 169–173. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450. 
  3. ^ Graham, D. E.; White, R. H. (2002). "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19: 133–147. doi:10.1039/b103714p. PMID 12013276. 
  4. ^ Rein, U.; Gueta, R.; Denger, K.; Ruff, J.; Hollemeyer, K.; Cook, A. M. (2005). "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA" (PDF). Microbiology. 151 (Pt 3): 737–747. doi:10.1099/mic.0.27548-0. PMID 15758220. 

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