Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: Analysis of volume changes upon reaction and hysteretic behavior

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1597, Issue 2, 2002, Pages 229-243

  Masson, Patrick ^a   Froment, Marie Thérèse ^a   Fort, Sébastien ^a   Ribes, Fabien ^a   Bec, Nicole ^b   Balny, Claude ^b   Schopfer, Lawrence M ^c  

^a CENTRE DE RECHERCHES   (France)

^b INSERM   (France)

^c UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Butyrylcholinesterase; Double mutant cycle; Hydrostatic pressure; Hysteresis; Lyotropic salt; Slow conformational change; Transient; Volume change

Indexed keywords

ACETIC ACID DERIVATIVE; BENZOYLCHOLINE; BUTYRYLTHIOCHOLINE; CHOLINESTERASE; N METHYLINDOXYL ACETATE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CALCULATION; CATALYST; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; HYDRATION; HYDROLYSIS; HYDROSTATIC PRESSURE; HYSTERESIS; MICHAELIS MENTEN KINETICS; MOLECULE; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ANIMALS; BUTYRYLCHOLINESTERASE; CATALYSIS; CATALYTIC DOMAIN; CHO CELLS; CRICETINAE; ENZYME ACTIVATION; HUMANS; HYDROLYSIS; HYDROSTATIC PRESSURE; INDOLES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SALTS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 0037013985     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(02)00265-0     Document Type: Article

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