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1.3.1.10: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

This is an abbreviated version!
For detailed information about enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific), go to the full flat file.

Word Map on EC 1.3.1.10

Reaction

acyl-[acyl-carrier protein]
+
NADP+
=
trans-2,3-dehydroacyl-[acyl-carrier protein]
 +
NADPH
 +
H+

Synonyms

1-cyclohexenylcarbonyl coenzyme A reductase, 2-enoyl thioester reductase, 2-trans-enoyl-ACP reductase, acyl-ACP dehydrogenase, beta-ketoacyl reductase, enoyl acyl-carrier-protein reductase, enoyl reductase, enoyl thioester reductase, enoyl-ACP reductase, enoyl-ACP reductase II, enoyl-ACP reductase III, enoyl-ACP-reductase II, enoyl-acyl carrier protein reductase, enoyl-[acyl carrier protein] reductase, enoyl-[acyl-carrier-protein] reductase, ENR, Etr1p, fabG4, FabI, FabK, FabL, Fabl2, More, Mrf1p, NADPH 2-enoyl Co A reductase, reductase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate), trans-enoyl-[acyl-carrier-protein] reductase, YgaA

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.10 enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

Crystallization

Crystallization on EC 1.3.1.10 - enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FabL in apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, X-ray diffraction structure determination and analysis
FabL in apo form and in the ternary complex with NADP+ and inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide, 8 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M sodium citrate pH 5.6, 8% w/v PEG 10,000 and 0.4 M magnesium acetate, hanging-drop methods, for the ternary BcFabL-NADP+-INH complex, NADP+ and inhibitor are added at the molar ratio of 1:1.5 and 1:5, respectively, equilibration in a stabilizing solution containing 0.1 M sodium citrate, pH 5.6, 8% w/v PEG 10,000, 0.4 M magnesium acetate with 30% v/v ethylene glycol as the cryoprotectant, X-ray diffraction structure determination and analysis at 2.2-3.0 A resolution
hanging drop vapour diffusion method with 0.04 M MgCl2, 0.05 M sodium cacodylate pH 6.0 and 11% (v/v) 2-methyl-2,4-pentanediol at 4°C
-
purified recombinant wild-type enzyme free and in complex with NADPH, mutant enzyme Y79N, hanging drop vapour diffusion method, 22°C, 15-25 mg/ml free enzyme in 50 mM sodium phosphate, pH 7.0, 150 mM NaCl with or without 10 mM NADPH, in a 1:1 ratio with reservoir solution containing 1.9 M ammonium sulfate, and 0.1 M N-(2-acetamido)-2-iminodiacetic acid/NaOH, at pH 6.5 for the free enzyme and pH 7.0 for the cofactor-complexed enzyme, mutant Y79N is crystallized using 15 mg/ml protein and reservoir solution at pH 7.0, labeling by soaking in heavy-atom-solutions, X-ray diffraction structure determination and analysis at 1.7 A, 2.25 A, and 2.6 A, respectively
-
structure to 1.9 A resolution with endogenous FMN fully resolved and the NADPH cofactor partially resolved. FabK possesses a TIM-barrel motif, and all flexible loops are visible