Investigation of mechanistic consequences of natural structural variation within the cysteine proteinases by knowledge-based modelling and kinetic methods.
نویسندگان
چکیده
second contained the thiol-dependent activity towards this substrate. The active protein, separated from cysteine by gel filtration, was found to possess a key catalytic site characteristic that is typical of many cysteine proteinases [ 1, 2, IS]. Thus stopped-flow kinetic analysis of the reaction of its catalytically essential thiol group with 2-Py-S-S-2-Py showed that the reactivity is a minimum at a pH value of approx. 6 and increases at both lower and higher pH values (approx. 4 and X), behaviour characteristic of the presence of an S / -Im'H ion pair [2, IS].
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عنوان ژورنال:
- Biochemical Society transactions
دوره 18 4 شماره
صفحات -
تاریخ انتشار 1990