long-chain acyl-protein thioester reductase;
luxC (gene name);
acyl coenzyme A reductase;
long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming);
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
long-chain-aldehyde:NADP+ oxidoreductase (protein thioester-forming)
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+ [RN:
[protein]-S-(long-chain fatty acyl)-L-cysteine;
Together with a hydrolase component (EC
) and a synthetase component (EC
), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC
). The enzyme is acylated by receiving an acyl group from EC
, 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.
EC 188.8.131.52 created 1986, modified 2016
ec00073 Cutin, suberine and wax biosynthesis
ec01110 Biosynthesis of secondary metabolites
K03400 long-chain-fatty-acyl-CoA reductase
Genes » show all
Riendeau D, Rodriguez A, 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 257:6908-15 (1982)
Wall, L. and Meighen, E.A.
Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum.
Biochemistry 25:4315-4321 (1986)
Lin JW, Chao YF, Weng SF
Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi.
ExplorEnz - The Enzyme Database: 184.108.40.206
ExPASy - ENZYME nomenclature database: 220.127.116.11