PMID: 5414Sep 1, 1975

Elementary processes in the interaction of serine protease with a possible transition state analog. Subtillisin-benzeneboronic acid system

Journal of Biochemistry
H NakataniK Hiromi

Abstract

The interaction of benzeneboronic acid(BBA), a possible transition state analog, with subtilisin BPN' [EC 3.4.21.14] was studied by the temperature-jump method at various pH's, temperatures and in D2O as well as H2O. From analysis of the concentration dependence of the relaxation times, it was suggested that the subtillsin-BBA interactions consist of at least two elementary steps, a fast bimolecular association followed by a slow unimolecular process. Similar concentration dependence was observed at pH 6.1-6.7 at 25degrees. However, in D2O the reciprocal relaxation times generally decreased compared to those in H2O and became concentration-independent below pD 6.5. The relaxation times were influenced considerably by the temperature. From these results, the slow unimolecular process was assigned to the trigonal-tetrahedral interconversion of BBA at the active site of the enzyme.

Citations

Oct 12, 1981·FEBS Letters·M Philipp, S Maripuri
Jan 1, 1983·Molecular and Cellular Biochemistry·M Philipp, M L Bender
Feb 1, 1996·European Journal of Biochemistry·M L RemerowskiF J Van De Ven

Related Concepts

Benzene
Boronic Acids
Hydrogen-Ion Concentration
Mathematics
Peptide Hydrolases
Plasma Protein Binding Capacity
Subtilisin 72
Thermodynamics

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