EC number:1.3.1.104

Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.1 With NAD+ or NADP+ as acceptor
ID:1.3.1.104
Description:Enoyl-[acyl-carrier-protein] reductase.
Alternative Name: Enoyl-ACP reductase.
Acyl-ACP dehydrogenase.
Cath: 1.10.1200.10; 1.10.1470.20; 1.10.287.1960; 3.30.70.250; 3.30.70.3290; 3.40.50.720; 3.90.180.10; 3.40.366.10; 3.40.47.10; 3.40.50.1820;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.1.104
BRENDA Enzyme Link: BRENDA 1.3.1.104
KEGG Enzyme Link: KEGG1.3.1.104
BioCyc Enzyme Link: BioCyc 1.3.1.104
ExPASy Enzyme Link: ExPASy1.3.1.104
EC2PDB Enzyme Link: EC2PDB 1.3.1.104
ExplorEnz Enzyme Link: ExplorEnz 1.3.1.104
PRIAM enzyme-specific profiles Link: PRIAM 1.3.1.104
IntEnz Enzyme Link: IntEnz 1.3.1.104
MEDLINE Enzyme Link: MEDLINE 1.3.1.104

EC number:1.3.1.104

MSA:

1.3.1.104;
Phylogenetic Tree:

1.3.1.104;
Uniprot:
M-CSA:
RHEA:22564 a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Human fatty acid synthase: properties and molecular cloning.Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ1995 Sep 127567999
Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli.Saito K, Kawaguchi A, Seyama Y, Yamakawa T, Okuda S1981 Jun 17021150
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.Dugan RE, Slakey LL, Porter JW1970 Dec 104394955
Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase.Seyama Y, Kasama T, Yamakawa T, Kawaguchi A, Saito K1977 Nov338601
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.Kim KH, Ha BH, Kim SJ, Hong SK, Hwang KY, Kim EE2011 Feb 2521185310
Mechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureus.Xu H, Sullivan TJ, Sekiguchi J, Kirikae T, Ojima I, Stratton CF, Mao W, Rock FL, Alley MR, Johnson F, Walker SG, Tonge PJ2008 Apr 818335995
Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis.Kim KH, Park JK, Ha BH, Moon JH, Kim EE2007 Mar 117329825
Substrate recognition by the human fatty-acid synthase.Carlisle-Moore L, Gordon CR, Machutta CA, Miller WT, Tonge PJ2005 Dec 3016215233
Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers.Torkko JM, Koivuranta KT, Kastaniotis AJ, Airenne TT, Glumoff T, Ilves M, Hartig A, Gurvitz A, Hiltunen JK2003 Oct 1712890667
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.Heath RJ, Su N, Murphy CK, Rock CO2000 Dec 2211007778