Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain.

@article{Kowlessur1989IdentificationOS,
  title={Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain.},
  author={D. Kowlessur and C. Topham and E. Thomas and M. O'driscoll and W. Templeton and K. Brocklehurst},
  journal={The Biochemical journal},
  year={1989},
  volume={258 3},
  pages={
          755-64
        }
}
1. 2-(N'-Acetyl-L-phenylalanyl)hydroxyethyl 2'-pyridyl disulphide (compound V) was synthesized, and a study of the pH-dependence of the second-order rate constant (k) for its reaction with the catalytic-site thiol group of papain (EC 3.4.22.2) was used to evaluate the consequences for transition-state geometry of the presence of a hydrophobic occupant for the S2 subsite of the enzyme in the absence of the N-H component of the P1-P2 amide bond. 2. Comparison of the pH-dependences of K for… Expand
The contribution of intermolecular hydrogen bonding to the kinetic specificity of papain.
Catalytic mechanism in papain family of cysteine peptidases.
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