Temperature-jump Studies on Benzeneboronic Acid-Serine Protease Interactions

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Abstract
The interactions of benzeneboronic acid (BBA) as a transition state analog with subtilisin [EC 3.4. 21. 4] and with α-chymotrypsin [EC 3. 4. 21.1] were investigated kinetically by the temperature-jump method using pH indicators. For both enzymes, the concentration dependence of the relaxation time was consistent with a two-step mechanism involving a fast bimolecular association followed by a slow, unimolecular process. The possibility of a trigonal-tetrahedral interconversion of BBA at the active site of the enzyme is discussed.