Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDF-Reference-Cited by-同舟云学术

Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDF

Published:1998-06-26 Issue:29 Volume:37 Page:10507-10513
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nachon Florian¹,Ehret-Sabatier Laurence¹,Loew Damarys¹,Colas Christophe¹,van Dorsselaer Alain¹,Goeldner Maurice¹

Affiliation:

1. Laboratoire de Chimie Bio-organique, UMR 7514 CNRS, Faculté de Pharmacie, Université Louis Pasteur Strasbourg, 74 route du Rhin, BP 24, 67401 Illkirch Cedex, France, and Laboratoire de Spectrométrie de Masse Bio-organique, UMR 7509 CNRS, Faculté de Chimie, Université Louis Pasteur Strasbourg, 1 rue Blaise Pascal, 67096 Strasbourg Cedex, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi980536l

Reference41 articles.

1. Molecular and cellular biology of cholinesterases

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

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