Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates

Journal of Biochemical and Molecular Toxicology

Volumn 23, Issue 5, 2009, Pages 303-308

  Chiou, Shyh Ying ^a,b   Huang, Chuan Fu ^a,b   Hwang, Mei Ting ^c   Lin, Gialih ^c  

^a CHUNG SHAN MEDICAL UNIVERSITY HOSPITAL   (Taiwan)

^b CHUNG SHAN MEDICAL UNIVERSITY   (Taiwan)

^c NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Acetylcholinesterase; Butyrylcholinesterase; Carbamate; Conformation; Inhibitor

Indexed keywords

ACETYLCHOLINESTERASE; BENZENE 1,4 DI N HEXYLCARBAMATE; BENZENE 1,4 DI N OCTYLCARBAMATE; CARBAMIC ACID DERIVATIVE; CHOLINE ETHYLENE; CHOLINESTERASE; ENZYME INHIBITOR; ETHYLENE DERIVATIVE; N HEXYLCARBAMYL; N OCTYLCARBAMYL; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BOND; CHEMICAL STRUCTURE; CONFORMATION; CONTROLLED STUDY; ENZYME INHIBITION; ISOMER; SUBSTITUTION REACTION;

ACETYLCHOLINESTERASE; BENZENE; BINDING SITES; BUTYRYLCHOLINESTERASE; CARBAMATES; CHOLINESTERASE INHIBITORS; ISOMERISM; KINETICS; MODELS, CHEMICAL; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 70350153783     PISSN: 10956670     EISSN: 10990461     Source Type: Journal    
DOI: 10.1002/jbt.20286     Document Type: Article

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