Biology:Rubredoxin—NAD(+) reductase
| rubredoxin-NAD+ reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.18.1.1 | ||||||||
| CAS number | 9032-27-3 | ||||||||
| 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+ reductase (EC 1.18.1.1) is an enzyme that catalyzes the chemical reaction.
- 2 reduced rubredoxin + NAD+ + H+ [math]\displaystyle{ \rightleftharpoons }[/math] 2 oxidized rubredoxin + NADH
The 3 substrates of this enzyme are reduced rubredoxin, NAD+, and H+, whereas its two products are oxidized rubredoxin and NADH.
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+ oxidoreductase. Other names in common use include rubredoxin reductase, rubredoxin-nicotinamide adenine dinucleotide reductase, dihydronicotinamide adenine dinucleotide-rubredoxin reductase, reduced nicotinamide adenine dinucleotide-rubredoxin reductase, NADH-rubredoxin reductase, rubredoxin-NAD reductase, NADH: rubredoxin oxidoreductase, DPNH-rubredoxin reductase, and NADH-rubredoxin oxidoreductase. This enzyme participates in fatty acid metabolism. It has 2 cofactors: FAD and Iron.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1BFY.
References
- "Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation". J. Biol. Chem. 242 (19): 4334–40. 1967. PMID 4294330.
- "Enzymatic -oxidation. VI. Isolation of homogeneous reduced diphosphopyridine nucleotide-rubredoxin reductase". J. Biol. Chem. 247 (7): 2109–16. 1972. PMID 4335861.
- "Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation". J. Biol. Chem. 247 (16): 5010–6. 1972. PMID 4403503.
- "Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum". Biochem. Biophys. Res. Commun. 91 (4): 1258–65. 1979. doi:10.1016/0006-291X(79)91202-6. PMID 526302.
 |  |
