Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.

@article{Brocklehurst1988ConsequencesOM,
  title={Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.},
  author={K. Brocklehurst and D. Kowlessur and G. Patel and W. Templeton and K. Quigley and E. Thomas and C. Wharton and F. Willenbrock and R. J. Szawelski},
  journal={The Biochemical journal},
  year={1988},
  volume={250 3},
  pages={
          761-72
        }
}
1. The pH-dependences of the second-order rate constant (k) for the reactions of papain (EC 3.4.22.2) with 2-(acetamido)ethyl 2'-pyridyl disulphide and with ethyl 2-pyridyl disulphide and of k for the reaction of benzimidazol-2-ylmethanethiol (as a minimal model of cysteine proteinase catalytic sites) with the former disulphide were determined in aqueous buffers at 25 degrees C at I 0.1. 2. Of these three pH-k profiles only that for the reaction of papain with 2-(acetamido)ethyl 2'-pyridyl… Expand
Catalytic mechanism in papain family of cysteine peptidases.
Cysteinyl proteinases and their selective inactivation.
  • E. Shaw
  • Chemistry, Medicine
  • Advances in enzymology and related areas of molecular biology
  • 1990
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