Accumulation of Tetrahedral Intermediates in Cholinesterase Catalysis: A Secondary Isotope Effect Study

Author:

Tormos Jose R.1,Wiley Kenneth L.1,Wang Yi1,Fournier Didier1,Masson Patrick1,Nachon Florian1,Quinn Daniel M.1

Affiliation:

1. The University of Iowa, Department of Chemistry, Iowa City, Iowa 52242, United States, Différenciation Cellulaire et Croissance, INRA, 2 place Viala, 34060 Montpellier, France, and Centre de Recherches du Service de Santé Armées, Unité d’Enzymologie, BP 87-38702 La Tronche CEDEX, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Reference43 articles.

1. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

2. The catalytic acceleration effected by AChE is estimated by dividingkcat= 104s−1by the rate constant for neutral hydrolysis of ACh,kuncat= 8 × 10−10s−1, estimated by Schowen:

3. Schowen, R. L.InTransition States of Biochemical Processes;Gandour, R. D. and Schowen, R. L., Eds.Plenum Press:New York and London, 1978; pp85−88.

4. Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products

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