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1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase

This is an abbreviated version!
For detailed information about 3-oxoacyl-[acyl-carrier-protein] reductase, go to the full flat file.

Word Map on EC 1.1.1.100

Reaction

a (3R)-3-hydroxyacyl-[acyl-carrier protein]
+
NADP+
=
a 3-oxoacyl-[acyl-carrier protein]
+
NADPH
+
H+

Synonyms

3-ketoacyl acyl carrier protein reductase, 3-ketoacyl-(acyl-carrier-protein) reductase, 3-ketoacyl-ACP reductase, 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-ACP(CoA) reductase, 3-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-thioester reductase, 3-ketoacyl-[acyl-carrier-protein] reductase, 3-oxo-acyl-ACP reductase, 3-oxoacyl-(acyl carrier protein) reductase, 3-oxoacyl-(acyl-carrier-protein) reductase, 3-oxoacyl-ACP reductase, 3-oxoacyl-AcpM reductase, 3-oxoacyl-thioester reductase, 3-oxoacyl-[ACP]reductase, ACP reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl acyl carrier protein reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-(acyl carrier protein) reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, beta-ketoacyl-[acyl carrier protein] reductase, beta-ketoacyl-[acyl-carrier protein] (ACP) reductase, BKR, FabG, FabG1, FabG2, fabG3, fabG4, KACPR, KAR, KCR1, KCR2, ketoacyl-acyl carrier protein reductase, MabA, MSMEG_3150, MSMEG_6753, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, OAR, OAR1, Oar1p, PA4389, PA4786, PHA-specific acetoacetyl-CoA reductase, PhaB, pks3, polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase, reductase, 3-oxoacyl-[acyl carrier protein], RhlG, XCC0416

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase

Crystallization

Crystallization on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.8 A, determinantion of initial phases by molecular replacement
-
at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
Q81JG6
diffraction to 2.4 A. Final model contains two tetramers displaying 222 symmetry and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
Q81JG6
structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism
-
vapor diffusion method, using 0.1 M MES (pH 7.1), 1.6 M ammonium sulfate, and 10% (w/v) 1,4-dioxane
sitting drop vapor diffusion method, using 15-18% (w/v) PEG3350 and 0.4 M ammonium acetate in sodium acetate buffer at pH 5.0
in complex with hexanoyl-CoA, hanging drop vapor diffusion method, using
hanging drop vapor diffusion method, apoenzyme is crystallized by using 100 mM Na-HEPES (pH 7.5), 30% (w/v) PEG 400 and 200 mM magnesium chloride hexahydrate, while the complex with NADP+ is crystallized by using 200 mM sodium citrate tribasic dehydrate and 20% (w/v) PEG 3350
high-resolution crystal structures of the enzyme (MabA) in its apo, NADP+-bound and NADPH-bound forms. Crystals are grown in sitting drops in MR Crystallization Plates (Hampton Research) at 18°C
purified recombinant enzyme, vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 6.8, 0.5 M NaCl, 1 mM DTT, and 0.5 mM EDTA, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.0, 35% v/v 2-methyl-2,4-pentanediol, and 0.2 M LiSO4, equilibration against 1 ml of mother liquor, room temperature, 6 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified native and selenomethionine-labeled recombinant enzyme, hanging drop vapour diffusion method, 18°C, 2.5 mg/ml protein in 50 mm HEPES, pH 7.0, 5 mM Tris, pH 8.0, 0.15 mM ammonium sulfate, 6% PEG 4000, 0.1 M NaCl, 0.5 mM EDTA, and 0.5 mM DTT, mixed with reservoir solution containing 1 M HEPES, pH 7.0, 0.3 M ammonium sulfate, and 12% PEG 4000, plus 1 mM NADPH, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
crystalized at a resolution of 2.25 A
apo-form complexed with NADPH, vapor diffusion method, using 10% (w/v) polyethylene glycol 4000, 10% (v/v) 2-propanol, 0.1 M HEPES pH 7.0 and 30% (v/v) jeffamine ED2001, 0.1 M HEPES pH 7.5
hanging drop vapor diffusion method, using 2.0-2.7 M ammonium sulfate and 0.1 M Tris (pH 9.0)
-