Inactivation of proteases and esterases by halomethylated derivatives of dihydrocoumarins.

Abstract:

:A series of halomethylated derivatives of dihydrocoumarins has been found to inhibit irreversibly proteases and esterases. alpha-Chymotrypsin, subtilish, elastase are rapidly inactivated in the presence of these compounds, while trypsin, kallicrein, papain are inhibited more slowly. Esterases like acetylcholinesterase and butyrylcholinesterase also lose activity in their presence. Two structural features of these inactivators are essential for inhibition: a reactive cis-ester function and an alkylating function. Analogues of these derivatives having only one of these characteristics are inefficient. Therefore it is suggested that the efficiency of these bifunctional reagents is due to their character of potential "suicide substrates".

journal_name

Biochimie

journal_title

Biochimie

authors

Béchet JJ,Dupaix A,Roucous C,Bonamy AM

doi

10.1016/s0300-9084(77)80140-5

subject

Has Abstract

pub_date

1977-01-01 00:00:00

pages

241-6

issue

3

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(77)80140-5

journal_volume

59

pub_type

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