| EC |
1.1.1.337 |
| 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 |
| References: |
| 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15758220] |
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| [EC 1.1.1.337 created 2012] |
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