Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates

Biochemical Journal

Volumn 373, Issue 1, 2003, Pages 33-40

  Kovarik, Zrinka ^a,b   Radić, Zoran ^a   Berman, Harvey A ^c   Simeon Rudolf, Vera ^b   Reiner, Elsa ^b   Taylor, Palmer ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INSTITUTE FOR MEDICAL RESEARCH AND OCCUPATIONAL HEALTH   (Croatia)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

Acetylcholinesterase mutation; Butyrylcholinesterase mutation; Organophosphate inhibition; Stereoselectivity

Indexed keywords

CATALYSIS; CONFORMATIONS; REACTION KINETICS; STEREOCHEMISTRY;

STEADY-STATE KINETIC CONSTANTS;

BIOCHEMISTRY;

ACETYLCHOLINESTERASE; ALANINE; CHOLINESTERASE; GLUTAMINE; ISOLEUCINE; LEUCINE; METHYLPHOSPHONIC ACID; PHENYLALANINE; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INHIBITION; KINETICS; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; REACTION TIME; STEREOCHEMISTRY;

ACETYLCHOLINESTERASE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; BUTYRYLCHOLINESTERASE; CHOLINESTERASE INHIBITORS; HYDROLYSIS; KINETICS; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE LIBRARY; PHOSPHORIC ACID ESTERS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE DELETION;

EID: 0038682446     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021862     Document Type: Article

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