EC - Long-chain-fatty-acid—protein ligase

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IntEnz Enzyme Nomenclature


Accepted name:
long-chain-fatty-acid—protein ligase
Other names:
acyl-protein synthetase
luxE (gene name)
long-chain-fatty-acid—luciferin-component ligase
Systematic name:
long-chain-fatty-acid:protein ligase (AMP-forming)



Together with a hydrolase 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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047474
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: 6908-6915 (1982). [PMID: 7085612]
  2. Rodriguez, A., Meighen, E.
    Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria.
    J. Biol. Chem. 260: 771-774 (1985). [PMID: 3968067]
  3. Wall, L. and Meighen, E.A.
    Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum.
    Biochemistry 25: 4315-4321 (1986).
  4. Soly, R. R., Meighen, E. A.
    Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria.
    J. Mol. Biol. 219: 69-77 (1991). [PMID: 2023262]
  5. Lin, J. W., Chao, Y. F., 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: 764-773 (1996). [PMID: 8941351]

[EC created 1986, modified 2011, modified 2016]