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Temperature-jump Studies on the Interaction of Benzeneboronic Acid With Chymotrypsinogen

Temperature-jump Studies on the Interaction of Benzeneboronic Acid With Chymotrypsinogen

K Hanai

J Biochem. 1976 Sep;80(3):491-5.

PMID: 10289

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
LS793898	3-(N-propylaminocarbonyl)benzeneboronic acid			Price
LS793929	(4-allylaminocarbonyl)benzeneboronic acid			Price

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