The Reactant State for Substrate-Activated Turnover of Acetylthiocholine by Butyrylcholinesterase is a Tetrahedral Intermediate-Reference-Cited by-同舟云学术

The Reactant State for Substrate-Activated Turnover of Acetylthiocholine by Butyrylcholinesterase is a Tetrahedral Intermediate

Published:2005-09-30 Issue:42 Volume:127 Page:14538-14539
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tormos Jose R.¹,Wiley Kenneth L.¹,Seravalli Javier¹,Nachon Florian¹,Masson Patrick¹,Nicolet Yvain¹,Quinn Daniel M.¹

Affiliation:

1. Department of Chemistry, The University of Iowa, Iowa City, Iowa 52242, Centre de Recherches du Service de Santé Armées, Unité d'Enzymologie, BP 87-38702 La Tronche CEDEX, France, and Institut de Biologie Structurale, Laboratoire de Cristallographie et Cristallogénèse des Protéines, 38027 Grenoble, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja052401q

Reference11 articles.

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

2. The Cholinesterases: From Genes to Proteins

3. The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase

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

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