| rubredoxin—NAD(P)+ reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.18.1.4 | ||||||||
| CAS no. | 114514-31-7 | ||||||||
| 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 rubredoxin—NAD(P)+ reductase (EC 1.18.1.4) is an enzyme that catalyzes the chemical reaction
- reduced rubredoxin + NAD(P)+ oxidized rubredoxin + NAD(P)H + H+
The 3 substrates of this enzyme are reduced rubredoxin, NAD+, and NADP+, whereas its 4 products are oxidized rubredoxin, NADH, NADPH, and H+.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on iron-sulfur proteins as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is rubredoxin:NAD(P)+ oxidoreductase. Other names in common use include rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase, rubredoxin-nicotinamide adenine, dinucleotide phosphate reductase, NAD(P)+-rubredoxin oxidoreductase, and NAD(P)H-rubredoxin oxidoreductase. This enzyme participates in fatty acid metabolism.
References
- ^ Petitdemange H, Blusson H, Gay R (September 1981). "Detection of NAD(P)H--rubredoxin oxidoreductases in Clostridia". Analytical Biochemistry. 116 (2): 564–70. doi:10.1016/0003-2697(81)90403-6. PMID 6274224.
- ^ Ma K, Adams MW (September 1999). "A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus". Journal of Bacteriology. 181 (17): 5530–3. PMC 94068. PMID 10464233.
External links
- Rubredoxin---NAD(P)++reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This page was last edited on 26 August 2023, at 15:45