D-lactate dehydrogenase (cytochrome c-553)

D-lactate dehydrogenase (cytochrome c-553)
Identifiers
EC no.1.1.2.5
CAS no.37250-79-6
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

In enzymology, D-lactate dehydrogenase (cytochrome c-553) (EC 1.1.2.5) is an enzyme that catalyzes the chemical reaction

 
Fe3+
Fe2+
Fe3+
Fe2+
 
+ 2 H+
 

The substrate of this enzyme is (R)-lactic acid, which is acted on by two equivalents of the cofactor, ferrocytochrome c-553, which oxidises the hydroxy group to a keto group, giving pyruvic acid, while the cofactor's iron is reduced.[1][2]

This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (R)-lactate:ferricytochrome-c-553 2-oxidoreductase. This enzyme participates in pyruvate metabolism.

References

  1. ^ Enzyme 1.1.2.5 at KEGG Pathway Database.
  2. ^ Ogata, Mari; Arihara, Keiko; Yagi, Tatsuhiko (1981). "D-Lactate Dehydrogenase of Desulfovibrio vulgaris1". The Journal of Biochemistry. 89 (5): 1423–1431. doi:10.1093/oxfordjournals.jbchem.a133334. PMID 7275946.