IUBMB Enzyme Nomenclature


Accepted name: long-chain-fatty-acid—protein ligase

Reaction: ATP + a long-chain fatty acid + [protein]-L-cysteine = AMP + diphosphate + a [protein]-S-(long-chain-acyl)-L-cysteine

Other name(s): luxE (gene name); acyl-protein synthetase; long-chain-fatty-acid—luciferin-component ligase

Systematic name: long-chain-fatty-acid:protein ligase (AMP-forming)

Comments: Together with a transferase component (EC and a reductase 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 activates free long-chain fatty acids, generated by the action of the transferase component, forming a fatty acyl-AMP intermediate, followed by the transfer of the acyl group to an internal L-cysteine residue. It then transfers the acyl group to EC, long-chain acyl-protein thioester reductase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82657-98-5


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. Rodriguez, A. and Meighen, E. Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria. J. Biol. Chem. 260 (1985) 771-774. [PMID: 3968067]

3. Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315-4321.

4. Soly, R.R. and Meighen, E.A. Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria. J. Mol. Biol. 219 (1991) 69-77. [PMID: 2023262]

5. Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 228 (1996) 764-773. [PMID: 8941351]

[EC created 1986, modified 2011, modified 2016]

Return to EC 6.2.1 home page
Return to EC 6.2 home page
Return to EC 6 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page