Abstract
When the oxidation of D-phenylalanine by D-amino acid oxidase is measured in stopped-flow turnover experiments there is a lag in the formation of keto-phenylpyruvate which becomes progressively greater as the pH is raised from 6.5. Borohydride trapping experiments show that the transient accumulation of free imino acid largely accounts for the lag at pH 8.7. These results are consistent with the known hydrolytic behavior of imines.
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