Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.

@article{Brocklehurst1988SupracrystallographicRO,
  title={Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.},
  author={K. Brocklehurst and S. M. Brocklehurst and D. Kowlessur and M. O'driscoll and G. Patel and E. Salih and W. Templeton and E. Thomas and C. Topham and F. Willenbrock},
  journal={The Biochemical journal},
  year={1988},
  volume={256 2},
  pages={
          543-58
        }
}
1. The influence on the reactivities of the catalytic sites of papain (EC 3.4.22.2) and actinidin (3.4.22.14) of providing for interactions involving the S1-S2 intersubsite regions of the enzymes was evaluated by using as a series of thiol-specific two-hydronic-state reactivity probes: n-propyl 2-pyridyl disulphide (I) (a 'featureless' probe), 2-(acetamido)ethyl 2'-pyridyl disulphide (II) (containing a P1-P2 amide bond), 2-(acetoxy)ethyl 2'-pyridyl disulphide (III) [the ester analogue of probe… 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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