(R)-2-hydroxyacid dehydrogenase

In enzymology, a (R)-2-hydroxyacid dehydrogenase (EC 1.1.1.272) is an enzyme that catalyzes the chemical reaction

(R)-2-hydroxyacid dehydrogenase
Identifiers
EC no.1.1.1.272
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
(2R)-3-sulfolactate + NAD(P)+ 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

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

References

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  1. ^ 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 (13): 3688–92. doi:10.1128/JB.182.13.3688-3692.2000. PMC 94539. PMID 10850983.
  • 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.