Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisin in the catalytically relevant ionization state of

@article{Brocklehurst1981EvidenceTT,
  title={Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisin in the catalytically relevant ionization state of},
  author={K. Brocklehurst and J. P. Malthouse},
  journal={The Biochemical journal},
  year={1981},
  volume={193 3},
  pages={
          819-23
        }
}
The active centre of the semi-synthetic enzyme thiolsubtilisin was investigated by studying the kinetics of the reaction of the thiol group of cysteine-221 with the thiol-specific two-protonic-state reactivity probe 2,2'-dipyridyl disulphide. The three-states criterion [Brocklehurst (1974) Tetrahedron 30, 2397-2407] was used to provide definitive evidence of the existence of a thiol--imidazole interactive system in acidic media in which the sulphur atom possesses highly nucleophilic character… Expand
Two-protonic-state electrophiles as probes of enzyme mechanisms.
Kinetics of subtilisin and thiolsubtilisin
Computational design of catalytic dyads and oxyanion holes for ester hydrolysis.
Introduction of a cysteine protease active site into trypsin.
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