Abstract
The effect of pH on the hydrolysis of alpha-N-benzoyl-l-arginine ethyl ester (BAEE) and alpha-N-benzoyl-l-argininamide (BAA) by a proteolytic enzyme component purified from Ficus carica var. Kadota latex has been studied in detail over the pH range of 3 to 9.5. k(cat) (lim) values for the hydrolysis of BAEE and BAA were essentially identical (5.20 and 5.01 sec(-1), respectively at 30 degrees ). k(cat) values for hydrolysis of BAEE and BAA were dependent on prototropic groups with apparent pK values of 4.24 and 8.53 and 4.10 and 8.59, respectively. k(cat) (lim) values for tht hydrolysis of BAEE and BAA were essentially identical (5.20 and groups of pK 4.33 and 8.60 and 4.55 and 8.51, respectively. Thus the pH optimum is 6.5 for both substrates. K(m) (app) values for BAEE and BAA were 3.32 x 10(-2)m and 6.03 x 10(-2)m respectively over the pH range of 3.9 to 8.0. These data are interpreted in terms of the involvement of a carboxyl and a sulfhydryl group in the active center of the enzyme. The data do not support the concept that deacylation of the acyl-enzyme is completely the rate controlling step in the hydrolyses. Rather, it appears that the magnitude of k(2) and k(3) are not greatly different.
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