KEGG   ENZYME: 6.2.1.19Help
Entry
EC 6.2.1.19                 Enzyme                                 

Name
long-chain-fatty-acid---luciferin-component ligase;
acyl-protein synthetase
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 = AMP + diphosphate + an acyl-protein thioester [RN:R01407]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
long-chain fatty acid [CPD:C00638];
protein [CPD:C00017]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
acyl-protein thioester [CPD:C03371]
Comment
Together with EC 1.2.1.50 long-chain-fatty-acyl-CoA reductase, enzyme forms a fatty acid reductase system that produces the substrate of EC 1.14.14.3 alkanal monooxygenase (FMN-linked), thus being a component of the bacterial luciferase system.
History
EC 6.2.1.19 created 1986, modified 2011
Orthology
K06046  
long-chain-fatty-acid---luciferin-component ligase
Genes
PLU: 
plu2083(luxE)
PAY: 
PAU_02510(luxE)
VHA: 
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
  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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
82657-98-5

DBGET integrated database retrieval system