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EC Tree
IUBMB Comments 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, fatty-acid synthase system. 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).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-ACP dehydrogenase, enoyl-ACP reductase, enoyl-ACP reductase III, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, FabI, FabK, FabL, NADPH 2-enoyl Co A reductase, PG1416,
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acyl-ACP dehydrogenase
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enoyl-ACP reductase
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enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase
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NADPH 2-enoyl Co A reductase
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enoyl-ACP reductase III
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enoyl-ACP reductase III
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FabK
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FabL
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PG1416
locus name
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acyl-[acyl-carrier protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
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acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
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, fatty-acid synthase system. 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).
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37251-09-5
not distinguished from EC 1.3.1.10
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crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
additional information
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crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
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crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
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crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
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crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
Pigeon
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crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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Pigeon
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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?
additional information
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Pigeon
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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additional information
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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?
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NADPH
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panosialin A
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin B
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wA
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wB
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
pyridoxal 5'-phosphate
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4 mM at 30°C for 15 min on complete fatty acid synthase selectively and completely inactivates
triclosan
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triclosan
affinity varies with pH-value
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0.0478
crotonyl-CoA
pH 7.5, 25°C
additional information
additional information
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NADP+ binds to enzyme in anti conformation both between nicotinamide-ribose and adenine-ribose
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0.0043
panosialin A
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.0053
panosialin B
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.003
panosialin wA
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.0046
panosialin wB
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.00066
triclosan
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
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isoform FabL
UniProt
brenda
isoform FabL
UniProt
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guinea pig
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brenda
chicken
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brenda
Pigeon
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brenda
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UniProt
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UniProt
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rat
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brenda
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UniProt
brenda
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brenda
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as there is no information concerning the stereochemistry of hydrogen transfer from NADPH to substrate an appointment to EC 1.3.1.10 or EC 1.3.1.39 is impossible for the enzyme of this source
brenda
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brenda
Pigeon
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brenda
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brenda
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prepared of particle-free supernatant
brenda
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33090
x * 33090, calculated
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x * 33090, calculated
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x * 33090, calculated
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native enzyme and in complex with NADPH and inhibitor triclosan, to 2.8 A and 1.8 A resolution, respectively
apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation
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7.2
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activity of entire fatty acid synthase declined no more than 15% in 24 h at pH 7.2 in phosphate puffer
390763
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-20°C, 5 mg/ml concentration, 30% glycerol stock, stable for at least 1 month
-20C, 10 mM DTT
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expression in Escherichia coli
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analysis
sensitive assay method measuring the fluorescence decrease of NADPH as it is converted to NADP+ during the reaction, optimized for high-throughput screening
analysis
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sensitive assay method measuring the fluorescence decrease of NADPH as it is converted to NADP+ during the reaction, optimized for high-throughput screening
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Dugan, R.E.; Slakey, L.L.; Porter, J.W.
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
J. Biol. Chem.
245
6312-6316
1970
Pigeon, Rattus norvegicus
brenda
Leanz, G.F.; Hammes, G.G.
Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase
Biochemistry
25
5617-5624
1986
Gallus gallus
brenda
Seyama, Y.; Otsuka, H.; Kawaguchi, A.; Yamakawa, T.
Fatty acid synthetase from the Harderian gland of guinea pig: biosynthesis of methyl-branched fatty acids
J. Biochem.
90
789-797
1981
Cavia porcellus
brenda
Kwon, Y.J.; Sohn, M.J.; Oh, T.; Cho, S.N.; Kim, C.J.; Kim, W.G.
Panosialins, inhibitors of enoyl-ACP reductase from Streptomyces sp. AN1761
J. Microbiol. Biotechnol.
23
184-188
2013
Staphylococcus aureus (Q6GI75)
brenda
Kim, K.H.; Ha, B.H.; Kim, S.J.; Hong, S.K.; Hwang, K.Y.; Kim, E.E.
Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
J. Mol. Biol.
406
403-415
2011
Bacillus subtilis (P71079), Bacillus subtilis 168 (P71079)
brenda
Hevener, K.E.; Mehboob, S.; Boci, T.; Truong, K.; Santarsiero, B.D.; Johnson, M.E.
Expression, purification and characterization of enoyl-ACP reductase II, FabK, from Porphyromonas gingivalis
Protein Expr. Purif.
85
100-108
2012
Porphyromonas gingivalis (Q7MAW0), Porphyromonas gingivalis W83 (Q7MAW0)
brenda
Priyadarshi, A.; Kim, E.; Hwang, K.
Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP end triclosan
Proteins Struct. Funct. Bioinform.
78
480-486
2010
Staphylococcus aureus (Q6GI75)
brenda
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