Sep 1, 1976

Temperature-jump studies on the interaction of benzeneboronic acid with chymotrypsinogen

Journal of Biochemistry
K Hanai

Abstract

The interaction of chymotrypsinogen A with benzeneboronic acid (BBA), a transition state along inhibitor of serine proteases, was investigated by the temperature-jump method using pH indicators. It was found that l/tau is dependent on BBA concentration, in contrast to the case of the alpha-chymotrypsin [EC 3.4.21.1]-BBA system in which l/tau is independent of BBA concentration. By examination of the pH dependences of the kinetic parameters, the acid dissociation behavior of His 57 in chymotrypsinogen, chymotrypsinogen-trigonal BBA complex and chymotrypsinogen-tetrahedral BBA complex was analyzed. The kinetic deuterium isotope effect was also examined and found to occur principally on the acid dissociation constants. The state of the catalytic residues in the zymogen molecule is discussed based on these results.

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Mentioned in this Paper

Benzeneboronic acid
Study
Chymotrypsinogen A
Cathepsin G
Alpha-chymotrypsin
Serine Endopeptidases
Deuterium
Tau Proteins
D-glucofuranose cyclic 1,2-3,5 bis(butylboronate)-6-acetate
Serine Proteases

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