Formate dehydrogenase (cytochrome)
| formate dehydrogenase (cytochrome) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.2.1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a formate dehydrogenase (cytochrome) (EC 1.2.2.1) is an enzyme that catalyzes the chemical reaction
- formate + 2 ferricytochrome b1
CO2 + 2 ferrocytochrome b1 + 2 H+
Thus, the two substrates of this enzyme are formate and ferricytochrome b1, whereas its 3 products are CO2, ferrocytochrome b1, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
- Gale EF (1939). "Formic dehydrogenase of Bacterium coli: its inactivation by oxygen and its protection in the bacterial cell". Biochem. J. 33: 1012–1027.