KEGG   ENZYME: 6.2.1.19Help
Entry
EC 6.2.1.19                 Enzyme                                 

Name
long-chain-fatty-acid---protein ligase;
luxE (gene name);
acyl-protein synthetase;
long-chain-fatty-acid---luciferin-component ligase
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
long-chain-fatty-acid:protein ligase (AMP-forming)
Reaction(IUBMB)
ATP + a long-chain fatty acid + [protein]-L-cysteine = AMP + diphosphate + a [protein]-S-(long-chain-acyl)-L-cysteine [RN:R01407]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
long-chain fatty acid [CPD:C00638];
[protein]-L-cysteine [CPD:C02743]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
[protein]-S-(long-chain-acyl)-L-cysteine [CPD:C03371]
Comment
Together with a hydrolase component (EC 3.1.2.2/EC 3.1.2.14) and a reductase component (EC 1.2.1.50), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). 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 1.2.1.50, long-chain acyl-protein thioester reductase.
History
EC 6.2.1.19 created 1986, modified 2011, modified 2016
Orthology
K06046  
long-chain-fatty-acid---luciferin-component ligase
Genes
PLU: 
plu2083(luxE)
PAY: 
PAU_02510(luxE)
PTT: 
VHA: 
VCA: 
VFI: 
VF_A0919(luxE)
VFM: 
VSA: 
SWD: 
VEI: 
BMD: 
MAB: 
MMV: 
NBR: 
 » show all
Taxonomy
Reference
1  [PMID:7085612]
  Authors
Riendeau D, Rodriguez A, Meighen E.
  Title
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex.
  Journal
J. Biol. Chem. 257 (1982) 6908-15.
Reference
2  [PMID:3968067]
  Authors
Rodriguez A, Meighen E
  Title
Fatty acyl-AMP as an intermediate in fatty acid reduction to aldehyde in luminescent bacteria.
  Journal
J. Biol. Chem. 260 (1985) 771-4.
Reference
3
  Authors
Wall, L. and Meighen, E.A.
  Title
Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum.
  Journal
Biochemistry 25 (1986) 4315-4321.
Reference
4  [PMID:2023262]
  Authors
Soly RR, Meighen EA
  Title
Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria.
  Journal
J. Mol. Biol. 219 (1991) 69-77.
Reference
5  [PMID:8941351]
  Authors
Lin JW, Chao YF, Weng SF
  Title
Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi.
  Journal
Biochem. Biophys. Res. Commun. 228 (1996) 764-73.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
82657-98-5

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