The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism.

@article{Kurz1992TheRO,
  title={The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism.},
  author={Linda C Kurz and L Moix and Matthew Riley and Carl Frieden},
  journal={Biochemistry},
  year={1992},
  volume={31 1},
  pages={39-48}
}
We have previously shown that purine riboside, when bound to adenosine deaminase, forms a complex in which C-6 of the purine is tetrahedral [Kurz, L. C., & Frieden, C. (1987) Biochemistry 26, 8450]. We now report the rates of formation of enzyme-inhibitor complexes of two types, those which do and those which do not form such tetrahedral intermediates. In both cases, the rates are encounter-controlled since the progress curves for formation of the complexes are well-described by a simple second… CONTINUE READING

From This Paper

Topics from this paper.