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 the active centre by use of a two-protonic-state reactivity probe.

Ítems similars

• Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.
  per: Brocklehurst, K, et al.
  Publicat: (1981)
• Reactivities of the various protonic states in the reactions of papain and of L-cysteine with 2,2'- and with 4,4'- dipyridyl disulphide: evidence for nucleophilic reactivity in the un-ionized thiol group of the cysteine-25 residue of papain occasioned by its interaction with the histidine-159-asparagine-175 hydrogen-bonded system.
  per: Brocklehurst, K, et al.
  Publicat: (1972)
• The hydrophobic character of thiol-activated cytolysins
  per: Johnson, Mary K., et al.
  Publicat: (1982)
• Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin
  per: Kahyaoglu, Ara, et al.
  Publicat: (2002)
• Reactivities of neutral and cationic forms of 2,2'-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe.
  per: Brocklehurst, K, et al.
  Publicat: (1979)