KEGG   ENZYME: 1.2.1.50Help
Entry
EC 1.2.1.50                 Enzyme                                 

Name
long-chain-fatty-acyl-CoA reductase;
acyl-CoA reductase;
acyl coenzyme A reductase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming)
Reaction(IUBMB)
a long-chain aldehyde + CoA + NADP+ = a long-chain acyl-CoA + NADPH + H+ [RN:R02620]
Reaction(KEGG)
R02620;
(other) R10549
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Substrate
long-chain aldehyde [CPD:C00609];
CoA [CPD:C00010];
NADP+ [CPD:C00006]
Product
long-chain acyl-CoA [CPD:C02843];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Together with EC 6.2.1.19 long-chain-fatty-acid---luciferin-component ligase, forms a fatty acid reductase system that produces the substrate of EC 1.14.14.3 alkanal monooxygenase (FMN-linked), thus being part of the bacterial luciferase system.
History
EC 1.2.1.50 created 1986
Pathway
Cutin, suberine and wax biosynthesis
Biosynthesis of secondary metabolites
Orthology
K03400  
long-chain-fatty-acyl-CoA reductase
Genes
PLU: 
plu2079(luxC)
PAY: 
PAU_02514(luxC)
PTT: 
VHA: 
VCA: 
VFI: 
VF_A0923(luxC)
VFM: 
VSA: 
SWD: 
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: 
50936-56-6

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