In enzymology, a formate dehydrogenase (NADP+) (EC 1.17.1.10) is an enzyme that catalyzes the chemical reaction
| formate dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.1.10 | ||||||||
| CAS no. | 51377-43-6 | ||||||||
| 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 | ||||||||
| |||||||||
- formate + NADP+ CO2 + NADPH
Thus, the two substrates of this enzyme are formate and NADP+, whereas its two products are CO2 and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formate:NADP+ oxidoreductase. Other names in common use include NADP+-dependent formate dehydrogenase, and formate dehydrogenase (NADP+). This enzyme participates in methane metabolism. It has 3 cofactors: iron, Tungsten, and Selenium.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GSD.
References
edit- Andreesen JR, Ljungdahl LG (1974). "Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: purification and properties". J. Bacteriol. 120 (1): 6–14. doi:10.1128/JB.120.1.6-14.1974. PMC 245723. PMID 4154039.
- Yamamoto I, Saiki T, Liu SM, Ljungdahl LG (1983). "Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein". J. Biol. Chem. 258 (3): 1826–32. doi:10.1016/S0021-9258(18)33062-X. PMID 6822536.
