The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.

@article{Kowlessur1989TheIO,
  title={The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.},
  author={D. Kowlessur and M. O'driscoll and C. Topham and W. Templeton and E. Thomas and K. Brocklehurst},
  journal={The Biochemical journal},
  year={1989},
  volume={259 2},
  pages={
          443-52
        }
}
1. The pH-dependence of the second-order rate constant (k) for the reaction of actinidin (EC 3.4.22.14) with 2-(N'-acetyl-L-phenylalanylamino)ethyl 2'-pyridyl disulphide was determined and the contributions to k of various hydronic states were evaluated. 2. The data were used to assess the consequences for transition-state geometry of providing P2/S2 hydrophobic contacts in addition to hydrogen-bonding opportunities in the S1-S2 intersubsite region. 3. The P2/S2 contacts (a) substantially… Expand
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The dipole moment of cytochrome c.
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