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evolution
the enzyme protein contains conserved domains of KAS-I and II, elongating condensing enzymes, condensing enzymes superfamily, and 3-oxoacyl-[ACP] synthase II. Comparisons of Elaeis oleifera and Elaeis guineensis enzymes, overview
evolution
the enzyme protein contains conserved domains of KAS-I and II, elongating condensing enzymes, condensing enzymes superfamily, and 3-oxoacyl-[ACP] synthase II. Comparisons of Elaeis oleifera and Elaeis guineensis enzymes, overview
malfunction
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endogenous H2O2 (mainly produced by pyruvate oxidase) inhibits FabF activity by specifically oxidizing its active site cysteine-thiol residue
malfunction
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KASII inhibition does not significantly influence the wax ester and triacylglycerol levels in the plant, but the the C16/C18 ratio is significantly increased in total lipid extracts of leaf tissue when KASIIRNAi-3 is expressed with or without wax ester biosynthesis gene
metabolism
KAS-II enzyme catalyzes the elongation of C16:0-ACP to C18:0-ACP in plastidial fatty acid biosynthesis pathway
metabolism
rate-limiting KAS-II enzyme catalyzes the elongation of C16:0-ACP to C18:0-ACP in plastidial fatty acid biosynthesis pathway
metabolism
Q7CJ22
the beta-ketoacyl-acyl carrier protein (ACP) synthases, FabB, FabF, and FabH, catalyse the Claisen condensation of fatty acyl-thioesters and malonyl-ACP to form a 3-oxoacyl-ACP intermediate elongated by two carbon atoms. The initial cycle of elongation is catalysed by FabH, involving condensation of malonyl-ACP and acetyl-CoA, while subsequent cycles of elongation are performed by FabB or FabF
metabolism
the enzyme is involved in fatty-acid biosynthesis
metabolism
enzyme overexpression increases pinocembrin production in recombinant Escherichia coli
physiological function
KAS2 is necessary for embryo development
physiological function
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encoded in the gene cluster required for biosynthesis of the calcium dependent antibiotics
physiological function
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fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis
physiological function
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fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis
physiological function
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fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis. All FASII systems have initiation and elongation condensing enzymes which can catalyze the Claisen condensation of an acyl donor and malonyl-ACP to form a beta-ketoacyl-ACP
physiological function
the enzyme is involved in fatty-acid biosynthesis
physiological function
the level of the C16:0 in palm oil is dependent on the palmitoyl-acyl carrier protein [ACP] thioesterase, EC 3.1.2.14, and beta-ketoacyl-[ACP] synthase-II, EC 2.3.1.179, enzymes efficiency. Palm oil obtained from Elaeis guineensis contains about 44% palmitic acid
physiological function
the level of the C16:0 in palm oil is dependent on the palmitoyl-acyl carrier protein [ACP] thioesterase, EC 3.1.2.14, and beta-ketoacyl-[ACP] synthase-II, EC 2.3.1.179, enzymes efficiency. Palm oil obtained from Elaeis oleifera contains about 25% palmitic acid
additional information
active site structure of wild-type and mutant enzymes, ligand binding structures, overview
additional information
Q7CJ22
enzyme structure and active site architecture, comparison with FabH, EC 2.3.1.180. Substrate binding is controlled by residue Phe401
additional information
enzyme three-dimensional structure determination, molecular dynamics simulation, and comparison with the enzyme structure of Elaeis guineensis KASII, as well as with Streptococcus pneumonia KASII and Brucella melitensis KASII structures, molecular homology modelling, overview. Active sites of EoKASII are Cys316, His453, and His489
additional information
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enzyme three-dimensional structure determination, molecular dynamics simulation, and comparison with the enzyme structure of Elaeis guineensis KASII, as well as with Streptococcus pneumonia KASII and Brucella melitensis KASII structures, molecular homology modelling, overview. Active sites of EoKASII are Cys316, His453, and His489
additional information
enzyme three-dimensional structure determination, molecular dynamics simulation, and comparison with the enzyme structure of Elaeis oleifera KASII, as well as with Streptococcus pneumonia KASII and Brucella melitensis KASII structures, molecular homology modelling, overview. Active site residues of EgKASII are Cys316, His456, and His492
additional information
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enzyme three-dimensional structure determination, molecular dynamics simulation, and comparison with the enzyme structure of Elaeis oleifera KASII, as well as with Streptococcus pneumonia KASII and Brucella melitensis KASII structures, molecular homology modelling, overview. Active site residues of EgKASII are Cys316, His456, and His492
additional information
the enzyme has two active site His residues
additional information
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the enzyme has two active site His residues
additional information
the enzyme has two active site His residues
additional information
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the enzyme has two active site His residues