Investigation of mechanistic consequences of natural structural variation within the cysteine proteinases by knowledge-based modelling and kinetic methods.

نویسندگان

  • C M Topham
  • J Overington
  • D Kowlessur
  • M Thomas
  • E W Thomas
  • K Brocklehurst
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