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)⁺ ${\displaystyle \rightleftharpoons }$ 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.

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

• 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 (1): 169–73. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450.
• Graham DE, White RH (2002). "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19 (2): 133–47. doi:10.1039/b103714p. PMID 12013276.