Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket

Journal of Biological Chemistry

Volumn 268, Issue 23, 1993, Pages 17083-17095

  Ordentlich, A ^a   Barak, D ^a   Kronman, C ^a   Flashner, Y ^a   Leitner, M ^a   Segall, Y ^a   Ariel, N ^a   Cohen, S ^a   Velan, B ^a   Shafferman, A ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; BUTYRYLTHIOCHOLINE; CHOLINESTERASE; EDROPHONIUM; PROPIDIUM IODIDE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; HYDROPHOBICITY; PLASTICITY; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ACETYLCHOLINESTERASE; ALCOHOLS; ANIONS; BINDING SITES; BUTYRYLTHIOCHOLINE; CELL LINE; CHOLINESTERASE INHIBITORS; EDROPHONIUM; HUMAN; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROPIDIUM; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, NON-P.H.S.; THIOCHOLINE;

EID: 0027217179     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)