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(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
Search
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 edit

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

References edit

  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.


hydroxyacid, dehydrogenase, enzymology, enzyme, that, catalyzes, chemical, reactionidentifiersec, 272databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwaypriamprofilepdb, structuresrcsb, pdbe, pdbsumgene, on. In enzymology a R 2 hydroxyacid dehydrogenase EC 1 1 1 272 is an enzyme that catalyzes the chemical reaction R 2 hydroxyacid dehydrogenaseIdentifiersEC no 1 1 1 272DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins 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 Structural studies editAs of late 2007 only one structure has been solved for this class of enzymes with the PDB accession code 1RFM References edit 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 Portal nbsp Biology This EC 1 1 1 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title R 2 hydroxyacid dehydrogenase amp oldid 1172333878, wikipedia, wiki, book, books, library,

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