|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
|Photobacterium phosphoreum:||long-chain-fatty-acid--protein ligase: 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
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -2.4406128 [Latendresse13]
Enzyme Commission Summary:
Together with a transferase component ( EC 184.108.40.206/ EC 220.127.116.11) and a reductase component ( EC 18.104.22.168), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme ( EC 22.214.171.124).
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 126.96.36.199, long-chain acyl-protein thioester reductase.
Instance reactions of [a long-chain acyl-CoA + H2O → a long-chain fatty acid + coenzyme A + H+] (188.8.131.52):
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+ (184.108.40.206)
i3: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (220.127.116.11)
i4: palmitoleoyl-CoA + H2O → palmitoleate + coenzyme A + H+ (3.1.2.-)
i5: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (18.104.22.168)
i6: icosanoyl-CoA + H2O → arachidate + coenzyme A + H+ (22.214.171.124)
Relationship Links: BRENDA:EC:126.96.36.199, ENZYME:EC:188.8.131.52, IUBMB-ExplorEnz:EC:184.108.40.206, UniProt:RELATED-TO:P14286, UniProt:RELATED-TO:P29334, UniProt:RELATED-TO:Q51885, UniProt:RELATED-TO:Q52100, UniProt:RELATED-TO:Q56823
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
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