Kinetics of binding between thermolysin and Streptomyces metalloprotease inhibitor, talopeptin (MKI).

Abstract:

:The mechanism of binding between thermolysin with its specific inhibitor, talopeptin (MKI), was studied kinetically with the stopped-flow method by monitoring the enhancement of tryptophan fluorescence caused by the complex formation. Only one relaxation obeying first-order kinetics was observed. The dependence of the apparent first-order constant, kapp, on the inhibitor concentration is consistent with a minimum two-step mechanism, including a fast bimolecular binding step followed by a slow unimolecular step. It was found that the increase in tryptophan fluorescence occurs solely in the slow unimolecular step. The apparent second-order rate constant, (kon)app, in the low inhibitor concentration range, was determined over the pH range between 5 and 8.5 and decreases with increasing pH. The activation parameters for the overall binding process were obtained from the temperature dependence of (kon)app.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kitagishi K,Hiromi K

doi

10.1093/oxfordjournals.jbchem.a134177

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

55-9

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

93

pub_type

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