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Literature summary for 2.3.1.41 extracted from

  • von Wettstein-Knowles, P.; Olsen, J.G.; McGuire, K.A.; Henriksen, A.
    Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases (2006), FEBS J., 273, 695-710.
    View publication on PubMed
Search for more literature for 2.3.1.41

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and mutant enzymes, free or bound to C8 and C12, respectively, X-ray diffraction structure determination and analysis at 1.8-2.4 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
H298E site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.0–8.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure Escherichia coli
H298Q site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure Escherichia coli
K328A site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure Escherichia coli
K328E site-directed mutagenesis, the mutant is almost completely decarboxylation deficient Escherichia coli
K328F site-directed mutagenesis, the mutant is completely decarboxylation deficient Escherichia coli
K328H site-directed mutagenesis, the mutant is completely decarboxylation deficient Escherichia coli
K328I site-directed mutagenesis, the mutant is almost completely decarboxylation deficient Escherichia coli
K328R site-directed mutagenesis, the mutant is almost completely decarboxylation deficient, crystal structure determination with the free mutant enzyme, comparison to the wild-type enzyme structure Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] beta-ketoacyl-acyl-carrier protein synthase enzyme joins short carbon units to construct fatty acyl chains by a three-step Claisen condensation reaction, the reaction starts with a trans thioesterification of the acyl primer substrate from ACP to the enzyme, subsequently, the donor substrate malonyl-ACP is decarboxylated to form a carbanion intermediate, which in the third step attacks C1 of the primer substrate giving rise to an elongated acyl chain, H298 serves as a catalytic base in the decarboxylation step, the enzyme possesses a Cys-His-His catalytic triad, Lys328 has a dual role in catalysis: its charge influences acyl transfer to the active site Cys, and the steric restraint imposed on H333, as an obligate hydrogen bond donor at Ne, is of critical importance for decarboxylation activity, active sites of the wild-type KAS I, its H298 mutants, and their acyl complexes, overview Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 transfer of [3H]myristate from ACP to wild-type and Lys328 mutant KAS I Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Malonyl-CoA decarboxylation reaction Escherichia coli Acetyl-CoA + CO2
-
 ?
additional information enzyme active site structure of wild-type and mutants with or without bound C12 or C8, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More analysis of wild-type and mutant active sites with bound substrates at different pH, overview Escherichia coli

Synonyms

Synonyms Comment Organism
beta-ketoacyl-ACP synthase I
-
 Escherichia coli
Cys-His-His-type beta-ketoacyl-acyl carrier protein synthase
-
 Escherichia coli
KAS I
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 decarboxylation assay at, inactive at pH 4.0-5.0 Escherichia coli