The Enzyme Database

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Accepted name: long-chain acyl-protein thioester reductase
Reaction: a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
Other name(s): luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase
Systematic name: long-chain-aldehyde:NADP+ oxidoreductase (protein thioester-forming)
Comments: Together with a hydrolase component (EC and 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-56-6
1.  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]
2.  Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315–4321.
3.  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]
[EC created 1986, modified 2016]

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