| formate dehydrogenase (cytochrome) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Formate dehydrogenase-N hetero9mer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 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 / QuickGO | ||||||||
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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
CO2 + 2 ferrocytochrome b1 + 2 HThus, 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 (June 1939). "Formic dehydrogenase of Bacterium coli: its inactivation by oxygen and its protection in the bacterial cell". The Biochemical Journal. 33 (6): 1012–27. doi:10.1042/bj0331012. PMC 1264479. PMID 16746983.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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