D-lactate dehydrogenase (cytochrome)
| D-lactate dehydrogenase (cytochrome) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.2.4 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction
- (D)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c
Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (D)-lactate:ferricytochrome-c 2-oxidoreductase. Other names in common use include lactic acid dehydrogenase, D-lactate (cytochrome) dehydrogenase, cytochrome-dependent D-(−)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(−)-lactic cytochrome c reductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants[1] .[2] It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway
References
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- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
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