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.

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(CoA) reductase, 3-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-[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-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, beta-ketoacyl-[acyl carrier protein] reductase, beta-ketoacyl-[acyl-carrier protein] (ACP) reductase, BKR, FabG, FabG1, fabG4, KACPR, KCR1, KCR2, MabA, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, OAR, Oar1p, PHA-specific acetoacetyl-CoA reductase, PhaB, polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase, reductase, 3-oxoacyl-[acyl carrier protein], RhlG

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
-
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
-
structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism
-
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