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2.3.1.180: beta-ketoacyl-[acyl-carrier-protein] synthase III

This is an abbreviated version!
For detailed information about beta-ketoacyl-[acyl-carrier-protein] synthase III, go to the full flat file.

Word Map on EC 2.3.1.180

Reaction

acetyl-CoA
+
a malonyl-[acyl-carrier protein]
=
an acetoacetyl-[acyl-carrier protein]
 +
CoA
 +
CO2

Synonyms

3-ketoacyl ACP synthase III, 3-ketoacyl acyl carrier protein synthase III, 3-ketoacyl carrier protein synthase III, 3-ketoacyl-(acyl carrier protein) synthase IIIA, 3-ketoacyl-(acyl carrier protein) synthase IIIB, 3-ketoacyl-ACP synthase III, 3-ketoacyl-acyl carrier protein synthase III, 3-ketoacyl-acyl-carrier protein synthase III, 3-oxoacyl-ACP synthase III, 3-oxoacyl-acyl carrier protein synthase III, 3-oxoacyl-[acyl-carrier-protein] synthase III, 3-oxoacyl:ACP synthase III, AbyA1, acetoacetyl-ACP synthase, acetyl-CoA:ACP transacylase, acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase, ACO synthase III, ACP synthase III, AknE2, AlnI, AsuC3, AsuC4, AviN, BenQ, beta-ketoacyl (acyl carrier protein) synthase III, beta-ketoacyl acyl carrier protein synthase III, beta-ketoacyl acyl-carrier protein synthase III, beta-ketoacyl-(ACP) synthase III, beta-ketoacyl-(acyl-carrier-protein) synthase III, beta-ketoacyl-ACP III, beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP synthase III, beta-ketoacyl-ACP synthase III-like protein, beta-ketoacyl-ACP-synthase III, beta-ketoacyl-acyl carrier protein (ACP) synthase III, beta-ketoacyl-acyl carrier protein synthase III, beta-ketoacyl-acyl carrier protein synthase-III, beta-ketoacyl-[acyl-carrier protein (ACP)] synthase III, beta-ketoacyl-[acyl-carrier-protein] synthase III, beta-ketoacyl:acyl carrier protein synthase III, beta-ketoacylacylcarrier protein synthase III, beta-ketobutyryl-ACP synthase, BomK, CalO4, CerJ, ChlB3, ChlB6, CorB, DarB, DpsC, ecFabH, ecKAS III, efFabH, EsmD1, EvrI, FabH, FabH1, FabH2, FabH3, FabHA, FabHB, fatty acid biosynthesis, enzyme H, fatty acid synthase type II condensing enzyme, FdmS, FrenI/FrnI, HedS, hiFabH, initiation ketosynthase, JcKAS III, KAS III, KAS III-like protein, KAS IIIA, KAS IIIB, KAS-III, KAS3a, KAS3b, KASIII, KijB, LstA, LstAB, LstB, mtFabH, MxnB, nmFabH, NphT7, NzsF, paFabH, PpyS, PqsBC, PqsD, PtmR, RedP, RevR, RkD, saFabH, SalQ/Orf12, short-chain condensing enzyme, spFabH, spyFabH, SsfN, TcsB, ThgI, TiaF, Tmn15, [acyl-carrier-protein] synthase III

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.180 beta-ketoacyl-[acyl-carrier-protein] synthase III

Crystallization

Crystallization on EC 2.3.1.180 - beta-ketoacyl-[acyl-carrier-protein] synthase III

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme or mutant enzymes C155A, C264A and C155A/C264A in complex with octanoyl-CoA, using PEG3350 as a precipitant and Tris HCl buffer (pH 7.0-8.0) and 0.1 M calcium acetate
-
purified recombinant free enzyme, hanging drop vapour diffusion method, 20 mg/ml protein at 15°C with 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% PEG 3350, enzyme mutant D36A/E37A with 2-[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxybenzoylamino]benzoic acid, in 25% PEG 3350, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
cyrstals of ecFabH and the ecFabH/methyl-CoA disulfide complex are obtained by the hanging drop method
-
enzyme in complex with inhibitor CoA methyldisulfide
purified FabH as apoenzyme or ligand-bound complex, X-ray diffraction structure determination and analysis at 1.46 A resolution
purified FabH as apoenzyme or with bound acetyl-CoA, structure and reaction mechanism modeling
-
purified FabH, sitting drop vapour diffusion method, 2 crystal forms
-
purified recombinant His-tagged, selenomethionine-labeled wild-type enzyme, hanging drop vapour diffusion method, 15 mg/ml protein in 20 mM Tris, pH 7.4, 1 mM EDTA, and 1 mM DTT, crystallization solution contains 1.8-2.0 M ammonium acetate, 2% PEG 400, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8-2.5 A resolution, modeling
-
purified recombinant selenomethionine-labeled enzyme, 0.002 ml of 13 mg/ml protein in 20 mM Tris, pH 7.5, 50 mM NaCl, 10 mM DTT, and 4 mM acetyl-CoA, versus 0.002 ml reservoir solution containing 12-14% PEG 4000, 40 mM Bis-Tris propane, pH 7.0, and 80 mM magnesium acetate, overnight, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
sitting-drop vapor-diffusion method, pH 9.0, 10% PEG 200, 18% PEG 8000
crystallization of the mtFabH/decyl-CoA disulfide is achieved using the hanging-drop vapour-diffusion technique. The active site cysteine in both subunits of the wild type mtFabH dimer is able to react with either a dodecanoyl-CoA substrate or a decyl-CoA disulfide inhibitor
-
hanging-drop vapor diffusion method, crystal structures of mtFabH and C112A mtFabH with 1
mapping of the Thr45 phosphorylation site on the mtFabH crystal structure, overview
purified FabH, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
purified recombinant enzyme in complex with lauroyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.3 A resolution, modeling
purified recombinant mutant enzymes R46A/R161A and W42A/R163A, 0.003 ml R46A/R161A solution containing 20 mg/ml protein, 20 mM Tris-HCl, pH 7.5, 0.5 M NaCl, 2 mM 2-mercaptoethanol, 10% glycerol, mixed with 0.001 ml of crystallization solution containing 0.1 M HEPES, pH 7.5, 10% v/v isopropyl alcohol, 20% w/v PEG 4000, for the W42A/R163A solution 0.002 ml of protein solution is mixed with 0.001 ml of crystallization solution containing 0.2 M ammonium sulfate, and 30% w/v PEG 8000, X-ray diffraction structure determination and analysis at 2.0-2.65 A resolution
15 mg/ml purified enzyme in 20 mM Tris, pH 8.0, 3 mM DTT, 100 mM NaCl, 10% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
purified recombinant His-tagged KASIII, by sitting-drop vapour-diffusion method, 4 mg/ml proteinin 25 mM Tris-HCl, pH 7.5, 20% glycerol, 3 mM 2-mercaptoethanol, 1 M NaCl is mixed with precipitatnt solution containing 0.1 M HEPES, pH 7.2, 30% PEG 6000, 5% 2-methyl-2,4-pentanediol and 3% D-galactose, X-ray diffraction structure determination and analysis at 2.05 A resolution
-
purified recombinant enzyme in apoform or as acetylated enzyme, hanging drop vapour diffusion technique, mixing of 0.0015 ml of 20 mg/ml protein solution with an equal amount of reservoir solution, containing 10% propan-2-ol, 0.1 M HEPES, pH 7.5, 15% glycerol, 24% PEG 4000, and equilibration against 0.3 ml of reservoir solution, 13°C, acetylated-YpFabH by co-crystallisation with acetyl-CoA at a molar ratio of 5:5:1 of acetyl-CoA-malonyl-CoA-YpFabH at 10 mg/ml protein, X-ray diffraction structure determination and analysis at 18-2.2 A resolution, molecular replacement using the enzyme structure of Escherichia coli, PDB ID 1HN9, as search model