Hydrogen dehydrogenase (NADP+)
| hydrogen dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.12.1.3 | ||||||||
| CAS no. | 9027-05-8 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a hydrogen dehydrogenase (NADP+) (EC 1.12.1.3) is an enzyme that catalyzes the chemical reaction
- H2 + NADP+ H+ + NADPH
Thus, the two substrates of this enzyme are H2 and NADP+, whereas its two products are H+ and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydrogen:NADP+ oxidoreductase. Other names in common use include NADP+-linked hydrogenase, NADP+-reducing hydrogenase, hydrogen dehydrogenase (NADP+), and simply hydrogenase (which is ambiguous).
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2AUV.
References
[edit]- de Luca G, de Philip P, Rousset M, Belaich JP, Dermoun Z (1998). "The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity". Biochem. Biophys. Res. Commun. 248 (3): 591–6. doi:10.1006/bbrc.1998.9022. PMID 9703971.
