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

BRENDA support

Literature summary for 2.3.1.180 extracted from

  • Davies, C.; Heath, R.J.; White, S.W.; Rock, C.O.
    The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli (2000), Structure, 8, 185-195.
    View publication on PubMed
Search for more literature for 2.3.1.180

Cloned(Commentary)

Cloned (Comment) Organism
gene fabH, expression of His-tagged wild-type and mutant enzymes in strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Protein Variants

Protein Variants Comment Organism
C112S site-directed mutagenesis, the mutant enzyme shows abolished condensation and transacylation activities, but 4fold increased decarboxylation activity compared to the wild-type enzyme Escherichia coli
H244A site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but 6fold increased transacylation activity compared to the wild-type enzyme Escherichia coli
N274A site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but about 20% increased transacylation activity compared to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information regulation by feedback inhibition Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + malonyl-[acyl-carrier protein] Escherichia coli regulation by feedback inhibition acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 catalytic reaction mechanism via a tetrahedral transition state, active site structure contains an oxyanion hole and a tunnel, catalytic residues are Cys112, His244, and Asn274, which are all required for condensation activity of the enzyme, additionally His244 and Asp274 are required for decarboxylation, Cys112 is essential for transacylation, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + malonyl-[acyl-carrier protein]
-
 Escherichia coli acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
acetyl-CoA + malonyl-[acyl-carrier protein] regulation by feedback inhibition Escherichia coli acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
additional information the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Escherichia coli
More two thirds of the monomer are a highly structured alpha/beta motif, secondary structure, overview Escherichia coli

Synonyms

Synonyms Comment Organism
beta-ketoacyl-acyl carrier protein synthase III
-
 Escherichia coli
beta-ketobutyryl-ACP synthase
-
 Escherichia coli
FabH
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli