KEGG   ENZYME: 1.3.1.39Help
Entry
EC 1.3.1.39                 Enzyme                                 

Name
enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific);
acyl-ACP dehydrogenase;
enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase;
NADPH 2-enoyl Co A reductase;
enoyl-ACp reductase;
enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific);
acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific);
enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific);
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
Reaction(IUBMB)
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ [RN:R01404]
Reaction(KEGG)
Substrate
acyl-[acyl-carrier protein] [CPD:C00173];
NADP+ [CPD:C00006]
Product
trans-2,3-dehydroacyl-[acyl-carrier protein] [CPD:C00693];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
History
EC 1.3.1.39 created 1986, modified 2013
Reference
1  [PMID:4394955]
  Authors
Dugan RE, Slakey LL, Porter JW.
  Title
Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis.
  Journal
J. Biol. Chem. 245 (1970) 6312-6.
Reference
2  [PMID:16215233]
  Authors
Carlisle-Moore L, Gordon CR, Machutta CA, Miller WT, Tonge PJ
  Title
Substrate recognition by the human fatty-acid synthase.
  Journal
J. Biol. Chem. 280 (2005) 42612-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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