Interaction of thiolsubtilisin with Streptomyces subtilisin inhibitor, SSI.

Abstract:

:Subtilisin BPN' was chemically converted to thiolsubtilisin and the interaction of this modified enzyme with Streptomyces subtilisin inhibitor (SSI) was examined. SSI competitively inhibited the esterolytic activity of thiolsubtilisin toward p-nitrophenyl acetate with a K1 value of 1.3 X 10(-5) M at pH 7.5 Spectrophotometric analysis of the interaction between SSI and the modified enzyme yielded a Kd value of 4 X 10(-5) M at pH 9.7. These values are about 10(5)-fold greater than the Kd value (less than 10(-9) M at pH 7.5) for the native enzyme. This indicates that the small change in the active site structure of subtilisin (Ser221 to Cys221) leads to a considerable decrease in the binding affinity (by about 6-7 kcal/mol) to SSI.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Fujiwara K,Inouye K,Tonomura B,Murao S,Tsuru D

doi

10.1093/oxfordjournals.jbchem.a131660

subject

Has Abstract

pub_date

1977-07-01 00:00:00

pages

125-30

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

82

pub_type

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