| hydrogen dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.12.1.2 | ||||||||
| 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 (EC 1.12.1.2) is an enzyme that catalyzes the chemical reaction
- H2 + NAD+ H+ + NADH
Thus, the two substrates of this enzyme are H2 and NAD+, whereas its two products are H+ and NADH.
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:NAD+ oxidoreductase. Other names in common use include H2:NAD+ oxidoreductase, NAD+-linked hydrogenase, bidirectional hydrogenase, and hydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism and methane metabolism. It has 6 cofactors: FAD, Iron, FMN, Flavin, Nickel, and Iron-sulfur.
References[edit]
- BONE DH, BERNSTEIN S, VISHNIAC W (1963). "Purification and some properties of different forms of hydrogen dehydrogenase". Biochim. Biophys. Acta. 67: 581–8. doi:10.1016/0006-3002(63)91868-7. PMID 13968752.
- Schneider K, Schlegel HG (1976). "Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16". Biochim. Biophys. Acta. 452 (1): 66–80. doi:10.1016/0005-2744(76)90058-9. PMID 186126.
