Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis.

@article{Zalatan2006AlkalinePM,
  title={Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis.},
  author={Jesse G. Zalatan and Daniel Herschlag},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 4},
  pages={1293-303}
}
Enzyme-catalyzed phosphoryl transfer reactions have frequently been suggested to proceed through transition states that are altered from their solution counterparts. Previous work with Escherichia coli alkaline phosphatase (AP), however, suggests that this enzyme catalyzes the hydrolysis of phosphate monoesters through a loose, dissociative transition state, similar to that in solution. AP also exhibits catalytic promiscuity, with a low level of phosphodiesterase activity, despite the tighter… CONTINUE READING
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