formate dehydrogenase (NADP+) | |||||||||
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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 | ||||||||
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In enzymology, a formate dehydrogenase (NADP+) (EC 1.17.1.10) 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. 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.
Other oxidoreductases (EC 1.15–1.21) | |
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1.15: Acting on superoxide as acceptor | |
1.16: Oxidizing metal ions | |
1.17: Acting on CH or CH2 groups | |
1.18: Acting on iron–sulfur proteins as donors | |
1.19: Acting on reduced flavodoxin as donor | |
1.20: Acting on phosphorus or arsenic in donors | |
1.21: Acting on X-H and Y-H to form an X-Y bond |
Enzymes | |
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