L-lactate dehydrogenase (cytochrome)

L-lactate dehydrogenase (cytochrome)
Identifiers
EC no.1.1.2.3
CAS no.9078-32-4
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, L-lactate dehydrogenase (cytochrome) (EC number 1.1.2.3) is an enzyme that catalyzes the chemical reaction

 
Fe3+
Fe2+
Fe3+
Fe2+
 
+ 2 H+
 

The substrate of this enzyme is (S)-lactic acid, which is acted on by two equivalents of the cofactor, ferricytochrome c, which oxidises the hydroxy group to a keto group, giving pyruvic acid, while the cofactor's iron is reduced.[1][2][3][4]

See also

References

  1. ^ Enzyme 1.1.2.3 at KEGG Pathway Database.
  2. ^ Appleby CA, Morton RK (March 1959). "Lactic dehydrogenase and cytochrome b2 of baker's yeast; purification and crystallization". Biochem. J. 71 (3): 492–9. doi:10.1042/bj0710492. PMC 1196822. PMID 13638255.
  3. ^ Appleby CA, Morton RK (November 1959). "Lactic dehydrogenase and cytochrome b2 of baker's yeast. Enzymic and chemical properties of the crystalline enzyme". Biochem. J. 73 (3): 539–50. doi:10.1042/bj0730539. PMC 1197094. PMID 13793977.
  4. ^ Bach SJ, Dixon M, Zerfas LG (1946). "Yeast lactic dehydrogenase and cytochrome b(2)". Biochem. J. 40 (2): 229–39. doi:10.1042/bj0400229. PMC 1258326. PMID 16747991.