Abstract
A modified spectrophotometric method for analyzing the enzymatic activty of the seru enzyme which catalyzes the hydrolysis of paraoxon (E-600) has been developed. It was found that the reaction is not subject to either substrate or product inhibition. Neither p-aminophenyldiethyl phosphate nor p-aminophenylpinacolyl methylphosphonate were substrates, but were competitive inhibitors with K 4 values of 1.02·10 −3 M and 4.4·10 −4 M, respectively. The enzyme active site is proposed to contain a hydrophobic region at the binding site and to require an electron withdrawing group in the substrate to ensure that cleavage occurs through the PO bond or to stabilize an anionic site at the active site.
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