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MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Photobacterium phosphoreum: long-chain-fatty-acid--protein ligaseInferred from experiment: luxE

In Pathway: bacterial bioluminescence

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: long-chain-fatty-acid--protein ligase

Enzyme Commission Synonyms: acyl-protein synthetase

Taxonomic Range: Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): -2.4406128Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Together with a transferase component ( EC 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.

Citations: [Riendeau82, Wall86, Lin96, Soly91, Rodriguez85 ]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [a long-chain acyl-CoA + H2O → a long-chain fatty acid + coenzyme A + H+] (
i1: docosapentaenoyl-CoA + H2O → (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentenoate + coenzyme A + H+ (3.1.2.-)

i2: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (

i3: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (

i4: palmitoleoyl-CoA + H2O → palmitoleate + coenzyme A + H+ (3.1.2.-)

i5: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (

i6: icosanoyl-CoA + H2O → arachidate + coenzyme A + H+ (

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:P14286, UniProt:RELATED-TO:P29334, UniProt:RELATED-TO:Q51885, UniProt:RELATED-TO:Q52100, UniProt:RELATED-TO:Q56823

Revised 10-Nov-2011 by Caspi R, SRI International


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lin96: Lin JW, Chao YF, Weng SF (1996). "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(3);764-73. PMID: 8941351

Riendeau82: Riendeau D, Rodriguez A, Meighen E (1982). "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(12);6908-15. PMID: 7085612

Rodriguez85: Rodriguez A, Meighen E (1985). "Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria." J Biol Chem 260(2);771-4. PMID: 3968067

Soly91: Soly RR, Meighen EA (1991). "Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria." J Mol Biol 219(1);69-77. PMID: 2023262

Wall86: Wall, L., Meighen, E.A. (1986). "Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum." Biochemistry 25: 4315-4321.

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Mon May 2, 2016, biocyc14.