(R)-2-hydroxyacid dehydrogenase

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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)+ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1RFM.

[edit] References

^ Graupner M, Xu H, White RH (2000). "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". J. Bacteriol. 182: 3688–92. doi:10.1128/JB.182.13.3688-3692.2000. PMID 10850983.

IUBMB entry for 1.1.1.272
BRENDA references for 1.1.1.272 (Recommended.)
PubMed references for 1.1.1.272
PubMed Central references for 1.1.1.272
Google Scholar references for 1.1.1.272
Graupner M, White RH (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: 169–73. PMID 11451450.
Graham DE, White RH (2002). "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19: 133–47. doi:10.1039/b103714p. PMID 12013276.