Biology:Formate dehydrogenase (acceptor)
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Short description: Enzyme
| Formate dehydrogenase (acceptor) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.99.33 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Formate dehydrogenase (acceptor) (EC 1.1.99.33, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with systematic name formate:acceptor oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- formate + acceptor [math]\displaystyle{ \rightleftharpoons }[/math] CO2 + reduced acceptor
Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer] transferring electrons to a hydrogenase.
References
- ↑ "Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component". The Journal of Biological Chemistry 265 (30): 18213–8. October 1990. doi:10.1016/S0021-9258(17)44740-5. PMID 2211698.
- ↑ "Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis". The Journal of Biological Chemistry 271 (14): 8095–100. April 1996. doi:10.1074/jbc.271.14.8095. PMID 8626495.
- ↑ "Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer". Biochemistry 37 (10): 3518–28. March 1998. doi:10.1021/bi972177k. PMID 9521673.
External links
- Formate+dehydrogenase+(acceptor) at the US National Library of Medicine Medical Subject Headings (MeSH)
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