Together with a hydrolase component (EC 188.8.131.52 and EC 184.108.40.206) and a synthetase component (EC 220.127.116.11), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 18.104.22.168). The enzyme is acylated by receiving an acyl group from EC 22.214.171.124, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
Riendeau, D., Rodrigues, A. and Meighen, E. Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. J. Biol. Chem.257 (1982) 6908–6915. [PMID: 7085612]
Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry25 (1986) 4315–4321.
Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun.191 (1993) 314–318. [DOI] [PMID: 8447834]