High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine

European Journal of Biochemistry

Volumn 270, Issue 2, 2003, Pages 315-324

  Masson, Patrick ^a   Nachon, Florian ^a,b   Bartels, Cynthia F ^b   Froment, Marie Therese ^a   Ribes, Fabien ^a   Matthews, Cedric ^a   Lockridge, Oksana ^b  

^a CENTRE DE RECHERCHES   (France)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Butyrylcholinesterase; Excess substrate activation; Mutant enzyme; PH dependence; Steady state kinetics

Indexed keywords

BUTYRYLCHOLINE; CHOLINESTERASE; HISTIDINE; MUTANT PROTEIN;

ACIDITY; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME SUBSTRATE; KINETICS; PH; PRIORITY JOURNAL; PROTON TRANSPORT; TITRIMETRY; WILD TYPE;

AMINO ACID SUBSTITUTION; AMINO ACIDS; BUTYRYLCHOLINESTERASE; BUTYRYLTHIOCHOLINE; HUMANS; HYDROGEN-ION CONCENTRATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037238060     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03388.x     Document Type: Article

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