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• W1979769088 abstract "Site-directed mutagenesis of Bacillus subtilis N7 α-amylase has been performed to evaluate the roles of the active site residues in catalysis and to prepare an active catalytic-site mutant that can form a stable complex with natural substrates. Mutation of Asp-176, Glu-208, and Asp-269 to their amide forms resulted in over a 15 000-fold reduction of its specific activity, but all the mutants retained considerable substrate-binding abilities as estimated by gel electrophoresis in the presence of soluble starch. Conversion of His-180 to Asn resulted in a 20-fold reduction of kcat with a 5-fold increase in Km for a maltopentaose derivative. The relative affinities for acarbose vs. maltopentaoe were also compared between the mutants and wild-type enzyme. The results are consistent with the roles previously proposed in Taka-amylase A and porcine pancreatic α-amylase based on their X-ray crystallographic analyses, although different pairs had been assigned as catalytic residues for each enzyme. Analysis of the residual activity of the catalytic-site mutant by gel electrophoresis has suggested that it derived from the wild-type enzyme contaminating the mutant preparations, which could not be removed by use of an acarbose affinity column; thus, these mutants are completely devoid of activity. The affinity-purified mutant proteins should be useful for elucidating the complete picture of the interaction of this enzyme with starch." @default.
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• W1979769088 date "1992-04-01" @default.
• W1979769088 modified "2023-10-15" @default.
• W1979769088 title "Site-directed mutagenesis of active site residues in Bacillus subtilis α-amylase" @default.
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• W1979769088 doi "https://doi.org/10.1016/0167-4838(92)90249-d" @default.
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