The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate

Journal of the American Chemical Society

Volumn 127, Issue 42, 2005, Pages 14538-14539

  Tormos, Jose R ^a   Wiley, Kenneth L ^a,d   Seravalli, Javier ^a,e   Nachon, Florian ^b   Masson, Patrick ^b   Nicolet, Yvain ^c   Quinn, Daniel M ^a  

^a E11 SSH   (United States)

^b CENTRE DE RECHERCHES   (France)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^d HARVARD UNIVERSITY   (United States)

^e UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLTHIOCHOLINE; CHOLINESTERASE;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; ENZYME ACTIVATION; ENZYME SUBSTRATE; HYDROLYSIS;

ACETYLTHIOCHOLINE; BUTYRYLCHOLINESTERASE; CATALYSIS; DEUTERIUM; KINETICS;

EID: 27144551946     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja052401q     Document Type: Article

References (11)

1. Abbreviations: AChE, acetylcholinesterase; ATCh, acetylthiocholine; BuChE, butyrylcholinesterase; BSA, bovine serum albumin; DTNB, 5,5′-dithiobis(2-nitrobenzoic acid); mA, milli-absorbance unit.
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