Formate dehydrogenase (NADP+)
| formate dehydrogenase (NADP+) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 1.2.1.43 | ||||||
| CAS number | 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 / EGO | ||||||
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In enzymology, a formate dehydrogenase (NADP+) (EC 1.2.1.43) is an enzyme that catalyzes the chemical reaction
- 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GSD.
References
- Andreesen JR, Ljungdahl LG (1974). "Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: purification and properties". J. Bacteriol. 120 (1): 6–14. PMC 245723. PMID 4154039. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=245723.
- 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. PMID 6822536.