The activated form of the mutationally altered alkaline phosphatase from Escherichia coli S-19 was found to be identical with the wild type enzyme with respect to the following properties: sedimentation coefficient, circular dichroic and optical rotatory dispersion spectra, heat stability, broad substrate specificity, Km for 4-nitrophenyl phosphate, and Ki for inorganic phosphate. But the turnover number of the mutant enzyme at pH 8.0 was only one-tenth of that of the wild type enzyme. Analysis of the mechanism of catalytic action by transient kinetics showed that the amino acid substitution causes a specific alteration in the rate of the conformation change during the turnover of the enzyme without apparently affecting any other process in the multistep pathway. The comparison of the kinetics of substrate hydrolysis by mutant and wild type enzymes permits one to distinguish between various proposals for the mechanism of alkaline phosphatase.
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Halford et al. (1972) studied this question.
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