D-lactate dehydrogenase (cytochrome c-553)
This January 2023 relies largely or entirely on a single source. (January 2023) |
D-lactate dehydrogenase (cytochrome c-553) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.2.5 | ||||||||
CAS no. | 37250-79-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a D-lactate dehydrogenase (cytochrome c-553) (EC 1.1.2.5) is an enzyme that catalyzes the chemical reaction
- (R)-lactate + 2 ferricytochrome c-553 pyruvate + 2 ferrocytochrome c-553
Thus, the two substrates of this enzyme are (R)-lactate and ferricytochrome c-553, whereas its two products are pyruvate and ferrocytochrome c-553.
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
[edit]- Ogata M, Arihara K, Yagi T. "D-Lactate dehydrogenase of Desulfovibrio vulgaris". J. Biochem. Tokyo: 1423–1431.