Inhibitors tethered near the acetylcholinesterase active site serve as molecular rulers of the peripheral and acylation sites

Journal of Biological Chemistry

Volumn 278, Issue 40, 2003, Pages 38948-38955

  Johnson, Joseph L ^a   Cusack, Bernadette ^a   Hughes, Thomas F ^a,c   McCullough, Elizabeth H ^a   Fauq, Abdul ^a   Romanovskis, Peteris ^b   Spatola, Arno F ^a,b   Rosenberry, Terrone L ^a  

^a MAYO CLINIC   (United States)

^b UNIVERSITY OF LOUISVILLE   (United States)

^c University of Florida ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; HYDROLYSIS; MOLECULAR BIOLOGY; MUTAGENESIS;

LIGANDS;

BIOCHEMISTRY;

9 [(4 METHANETHIOSULFONYLMETHYLPHENYLACETYL)GLYCYL 7' AMIDOHEPTYL]AMINO 1,2,3,4 TETRAHYDROACRIDINE; 9 [N GAMMA (BETA METHANETHIOSULFONYLPROPIONYL) GAMMA AMINOPROPYLAMINO]ACRIDINE; 9 [N GAMMA (N EPSILON BETA METHANETHIOSULFONYLPROPIONYL EPSILON AMINOCAPROYL) GAMMA AMINOPROPYLAMINO]ACRIDINE; ACETYLCHOLINESTERASE; ACRIDINE DERIVATIVE; AMMONIUM DERIVATIVE; CATION; CHOLINESTERASE INHIBITOR; CYSTEINE; LIGAND; METHANE; METHANETHIOSULFONYLETHYL 2 (TRIMETHYLAMMONIUM); METHANETHIOSULFONYLHEXYL 7 (TRIETHYLAMMONIUM); METHANETHIOSULFONYLPROPYL 3 (TRIETHYLAMMONIUM); ORGANOPHOSPHATE; RESIN; TACRINE DERIVATIVE; UNCLASSIFIED DRUG;

ACYLATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CALCULATION; CATALYSIS; COMPETITIVE INHIBITION; DISULFIDE BOND; DRUG IDENTIFICATION; DRUG PROTEIN BINDING; DRUG STRUCTURE; DRUG SYNTHESIS; ENZYME ACTIVE SITE; HYDROLYSIS; MOLECULAR MODEL; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

ACETYLCHOLINESTERASE; BINDING SITES; CATIONS; CYSTEINE; DISULFIDES; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; HYDROLYSIS; KINETICS; LIGANDS; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROPIDIUM; PROTEIN BINDING; RECOMBINANT PROTEINS; TACRINE;

EID: 0141866710     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M304797200     Document Type: Article

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