Ferredoxin—NAD(+) reductase

From Wikipedia, the free encyclopedia
  (Redirected from Ferredoxin-NAD+ reductase)
Jump to: navigation, search
Ferredoxin-NAD+ reductase
Identifiers
EC number 1.18.1.3
CAS number 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 / EGO

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

reduced ferredoxin + NAD+ \rightleftharpoons 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.