In enzymology, a ferredoxin–NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction:
| Ferredoxin-NAD+ reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.18.1.3 | ||||||||
| CAS no. | 39369-37-4 | ||||||||
| 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 | ||||||||
| |||||||||
- reduced ferredoxin + NAD+ oxidized ferredoxin + NADH + H+
Thus, the two substrates of this enzyme are reduced ferredoxin and NAD+, whereas its 3 products are oxidized ferredoxin, NADH, and H+. This enzyme participates in fatty acid metabolism.
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 is ferredoxin:NAD+ oxidoreductase. There are a variety of names in common use:
- ferredoxin–nicotinamide adenine dinucleotide reductase
- ferredoxin reductase
- NAD+-ferredoxin reductase
- ferredoxin–NAD+ reductase
- ferredoxin–linked NAD+ reductase
- ferredoxin–NAD reductase
When NAD molecule is in its reduced form, the enzyme is referred to as:
- NADH-ferredoxin oxidoreductase
- reduced nicotinamide adenine dinucleotide-ferredoxin
- NADH-ferredoxin reductase
- NADH flavodoxin oxidoreductase
- NADH2-ferredoxin oxidoreductase
Other enzymes in the family include:
- NADH-ferredoxin NAP reductase (component of naphthalene dioxygenase multicomponent enzyme system)
- NADH-ferredoxin TOL reductase (component of toluene dioxygenase)
Structural studies edit
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1KRH.
References edit
- Jungermann K, Thauer RK, Leimenstoll G, Decker K (1973). "Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia". Biochim. Biophys. Acta. 305 (2): 268–80. doi:10.1016/0005-2728(73)90175-8. PMID 4147457.
