The kinetics of phenylacetamide hydrolysis catalyzed by polyacrylamide gel-immobilized penicillinamidase were studied. The Km and Kp values obtained were compared to the literary data for the specific substrate--benzylpenicillin. It was shown that the type of inhibition by the reaction product was the same, whereas the efficiency of binding of phenylacetic acid depended on the substrate structure.
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