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J. Biochem, 1977, Vol. 81, No. 5 1269-1272
© 1977 Japanese Biochemical Society

research-article

Interaction of Asp. melleus Semi-Alkaline Protease with Benzeneboronic Acid

Hiroshi NAKATANI, Hideshi FUJIWAKE and Keitaro HIROMI

Department of Food Science & Technology, Faculty of Agriculture, Kyoto University Sakyo-ku, Kyoto, Kyoto 606

Benzeneboronic acid (BBA), a possible transition-state analog for serine proteases, was found to inhibit Asp. melleus semi-alkaline protease [EC 3.4.21. 15]. The pH dependence of inhibitor constants was studied by the pH-stat method using N-acetyl-L-tyrosine ethyl ester as a substrate at 25°C. From the pH dependence of the association constant (reciprocal inhibitor constant), a pK value of 6.6, which may be attributable to the catalytic histidine residue of the enzyme, was estimated. The BBA-enzyme interaction was studied kinetically by the temperature-jump method. Apparent association and dissociation rate constants were determined at pH 6.5.


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