Ferredoxin—NAD(+) reductase
Ferredoxin-NAD+ reductase | |||||||||
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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 | ||||||||
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In enzymology, a ferredoxin–NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction:
- 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.