Elementary Processes in the Interaction of Serine Protease with a Possible Transition State Analog Subtilisin-Benzeneboronic Acid System1
- 1 September 1975
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 78 (3) , 611-616
- https://doi.org/10.1093/oxfordjournals.jbchem.a130947
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 subtilisin-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 25°. 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 intercon version of BBA at the active site of the enzyme.Keywords
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