Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH)

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

Word Map on EC 1.3.1.9

Reaction

an acyl-[acyl-carrier protein]
+
NAD+
=
a trans-2,3-dehydroacyl-[acyl-carrier protein]
 +
NADH
 +
H+

Synonyms

2-trans enoyl-ACP-reductase, 2-trans enoyl-acyl carrier protein reductase, 2-trans-enoyl-ACP (CoA) reductase, 2-trans-enoyl-ACP reductase, 2-trans-enoyl-ACP(CoA) reductase, ACP reductase, BaENR, BMA0885, bsFabI, cold-shock induced protein 15, CSI15, EACP reductase, enoyl (acyl carrier protein) reductase, enoyl ACP reductase, enoyl acyl carrier protein reductase, enoyl acyl carrier protein reductase InhA, enoyl reductase, enoyl-ACP reductase, enoyl-ACP reductase I, enoyl-ACP reductase III, enoyl-ACP(CoA) reductase, enoyl-acyl carrier protein, enoyl-acyl carrier protein reductase, enoyl-acyl carrier protein reductase I, enoyl-reductase, enoyl-[acyl-carrier-protein] reductase, ENR, ENR1, ENR2, FabI, FabI-1, FabI-related enoyl-ACP reductase, FabI1, FabI2, FabK, Fabl1, Fabl2, FabMG, FabV, FAS-II enoyl reductase, FTT_0782, InhA, More, MtENR, MtInhA, NAD-dependent enoyl-ACP reductase, NADH-dependent enoyl reductase, NADH-dependent enoyl-ACP reductase, NADH-dependent enoyl-acyl carrier protein reductase, NADH-enoyl acyl carrier protein reductase, NADH-ENR, NADH-specific enoyl-ACP reductase, OsmC, PA2950, pfENR, reductase, enoyl-[acyl carrier protein], trans-enoyl-[acyl carrier protein] reductase, trans-enoyl-[acyl-carrier-protein] reductase, VEG241, vegetative protein 241, VF_0888, YP_4011

ECTree

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

Crystallization

Crystallization on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.7 A resolution, orthorhombic space group P21212, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07A
crystal structure at 1.72 A resolution, protein adopts a Rossmann fold. FabI/NADH crystal structure at 1.86 A resolution, the protein undergoes a large conformational change to participate in covering the NADH-binding pocket
apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, to 3.0 and 2.2 A resolution, respectively. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation
in complex with inhibiotrs triclosan and (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetra hydro-1,8-naphthyridin-3-yl)acrylamide, to 2.7 A and 1.3 A resolution, respectively
complexed with NAD+ or crotonyl-CoA, hanging drop vapor diffusion method
-
complexed with NAD+, NADH or thienodiazaborine, hanging drop vapor diffusion method
-
apoform and in complex with NAD+, hanging drop vapor diffusion method, using
complexed with NAD+ and triclosan, hanging drop vapor diffusion method
complexed with NAD+, hanging drop vapor diffusion method
-
crystals of FabI/NAD+ complex with (E)-N-methyl-N-(1-methyl-1H-indol-3-ylmethyl)-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthydrin-3-yl)acrylamide diffract to 2.3 A
-
hanging drop vapor diffusion method, using 100 mM citrate pH 7.0, 100 mM ammonium sulfate, 22% (w/v) PEG 3350
in complex with NAD+ and triclosan, to 2.1 A resolution. The substrate-binding loop, residues 191–205, undergoes a major conformational change upon binding to triclosan and forms a lid on top of the triclosan moiety and the nicotinamide group that shields them from the solvent
modeling of the structure
in complex with NAD+ and triclosan or diclosan
in the presence of NAD+ and triclosan, hanging drop vapor diffusion method
-
apoenzyme by the sitting drop vapor diffusion method using 100 mM sodium acetate, 100 mM MES pH 6.5 and 30% (w/v) polyethyleneglycol 400 or enzyme in complex with isoniazid, NAD+ or NADH by the hanging drop vapor diffusion method using 100 mM HEPES pH 7.5, 8-10% (w/v) 2-methyl-2,4-pentanediol, 50 mM sodium citrate pH 6.5
hanging drop vapor diffusion technique, formation of the ternary enzyme/NAD+x012-(o-tolyloxy)-5-hexylphenol complex
in complex with NAD and isoniazid, hanging drop vapour diffusion method,in 50 mM HEPES, pH 7.2, sodium citrate buffer and 5-10% 2-methyl-2,4-pentanediol
purified recombinant His-tagged InhA in a ternary complex with NAD+ and PT70, 10 mg/ml protein is combined with NAD and PT70 in a molar ratio of 1:5:200, mixing of euqual volumes of protein and reservoir solution, the latter containing 12-16% w/v PEG 4000, 1% DMSO, 100 mM N-(2-acetamido)iminodiacetic acid, pH 6.8, and 100-250 mM ammonium acetate, 22°C, 4 days, X-ray diffraction structure determination and analysis at 1.8-2.1 A resolution, modelling, overview
the crystal structure of the enzyme in complex with the inhibitor N-(4-methylbenzoyl)-4-benzylpiperidine reveals the binding mode of the inhibitor within the active site
wild-type enzyme, S94A, I47T and I21V mutants in complex with NADH at resolutions of 2.3 A, 2.2 A, 2.0 A, 1.9 A, respectively
-
as binary complex with NADH and as ternary complex with NAD+ and triclosan, crystals diffract to 2.5 A and 2.2 A, respectively
-
crystals are grown by hanging-drop vapour-diffusion, 0.0025 ml protein solution containing 12 mg/ml enzyme in 20 mM sodium/potassium phosphate, pH 8.0, 150 mM NaCl, 0.005 mM NAD+ and 0.006 mM triclosan are mixed with 0.0025 ml reservoir solution at 17°C, optimal reservoir solution contains 19.5% polyethylene glycol 3350 and 230 mM KI, crystals diffract to 2.2 A
-
in complex with isoniazid and NAD+, hanging drop vapour diffusion method in 2.4 M (NH4)2SO4, 0.1 M MES pH 5.6, at 16°C
-
in complex with NADH and inhibitors, hanging drop vapor diffusion method
molecular dynamics simulations of tetrameric enzyme in different states of cofactor and ligand binding. Simulations show fluctuations in the substrate-binding loop and provide data of the pocket volume
mutants A372M, K316A in cimolex with triclosan, to 2.5 and 2.05 A resolution, respectively. The enzyme has a conserved salt bridge which stabilizes the substrate binding loop and appears to be important for the active conformation
X-ray crystal structures of Plasmodium falciparum enzyme in complex with triclosan variants having different substituted and unsubstituted groups at different key functional locations. 4 and 2' substituted compounds have more interactions with the protein, cofactor, and solvents when compared with triclosan. Substitution at the 2' position of triclosan causes the relocation of a conserved water molecule, leading to an additional hydrogen bond with the inhibitor. 2' and 4' unsubstituted compounds show a movement away from the hydrophobic pocket to compensate for the interactions made by the halogen groups of triclosan
apoenzyme and in complex with NAD+ and triclosan, hanging drop vapor diffusion method, using 0.1 M sodium malonate pH 5.0, 10% (w/v) polyethylene glycol 3350
in complex with 1, hanging drop vapour diffusion method, with 0.1 M MES, pH 5.5-7.0, 0.1 M NH4Cl, 0.2 M CaCl2, 8-15% 2-methyl-2,4-pentanediol , 8-15% polyethyleneglycol 1000, and 5 mM dithiothreitol
SeMet-substituted crystals are grown by the hanging-drop vapour-diffusion method, diffraction data are collected to 2.00 A resolution
the crystal structure of enoyl-acyl carrier protein reductase is determined at 1.7 A, in complex with a phenylimidazole derivative inhibitor at 2.3 A
crystals of enoyl reductase in complex with NAD+ and triclosan, data are collected to beyond 2.6 A
-
enzyme in complex with NAD+ and 19, X-ray diffraction structure determination and analysis at 2.7 A resolution
homology modeling of structure
to 1.6 A resolution, space group P212121. The model consists of one monomer in the asymmetric unit which is composed of 13 alpha-helices and 11 beta-strands, representing a canonical Rossmann fold architecture. In addition to the conserved residues Y236 and K245 in the Y-X8-K motif, Y53, D111 and Y226 are key residues implicated in the reductase activity, and F113 and T276 are also important for enzyme function
hanging drop vapor diffusion method, using 150 mM (NH4)2SO4, 100 mM MES (pH 5.6-5.9), and 26.5-37.5% (w/v) PEG4000
in complex with NADH, and in complex with inhibitors 1-(2-chlorobenzyl)-4-hexylpyridin-2(1H)-one and 1-(3-amino-2-methylbenzyl)-4-hexylpyridin-2(1H)-one, to 0.92-1.54 A resolution. Without a substrate bound, it adopts a closed conformation that has to open to allow access of the enoyl substrate or an inhibitor