Biology:(R)-2-hydroxyacid dehydrogenase
| (R)-2-hydroxyacid dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.272 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a (R)-2-hydroxyacid dehydrogenase (EC 1.1.1.272) is an enzyme that catalyzes the chemical reaction
- (2R)-3-sulfolactate + NAD(P)+ [math]\displaystyle{ \rightleftharpoons }[/math] 3-sulfopyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are (2R)-3-sulfolactic acid, NAD+, and NADP+, whereas its 4 products are 3-sulfopyruvic acid, NADH, NADPH, and H+. This enzyme is important in the metabolism of archaea, particularly their biosynthesis of coenzymes such as coenzyme M, tetrahydromethanopterin and methanofuran.[1]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-2-hydroxyacid:NAD(P)+ oxidoreductase. Other names in common use include (R)-sulfolactate:NAD(P)+ oxidoreductase, L-sulfolactate dehydrogenase, ComC, and (R)-sulfolactate dehydrogenase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1RFM.
References
- ↑ "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". J. Bacteriol. 182 (13): 3688–92. 2000. doi:10.1128/JB.182.13.3688-3692.2000. PMID 10850983.
- "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 (1): 169–73. 2001. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450.
- "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19 (2): 133–47. 2002. doi:10.1039/b103714p. PMID 12013276.
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