Accommodation of physostigmine and its analogues by acetylcholinesterase is dominated by hydrophobic interactions

Biochemical Journal

Volumn 417, Issue 1, 2009, Pages 213-222

  Barak, Dov ^a   Ordentlich, Arie ^a   Stein, Dana ^a   Yu, Qian Sheng ^b   Greig, Nigel H ^b   Shafferman, Avigdor ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

^b NATIONAL INSTITUTE ON AGING   (United States)

Author keywords

Alzheimer's disease; Carbamate; Hydrophobic subsite; Non covalent inhibition; Oxyanion hole

Indexed keywords

ALZHEIMER'S DISEASE; CARBAMATE; HYDROPHOBIC SUBSITE; NON-COVALENT INHIBITION; OXYANION HOLE;

DRUG INTERACTIONS; ENZYMES; LIGANDS; ORGANIC COMPOUNDS; OXYGEN; POSITIVE IONS; REACTION RATES; STEREOSELECTIVITY;

HYDROPHOBICITY;

ACETYLCHOLINESTERASE; CYMSERINE; ESEROLINE; PHENSERINE; PHYSOSTIGMINE DERIVATIVE; PHYSOSTIGMINE SALICYLATE; PHYSOVENINE; PHYSOVENOL; PYRIDOSTIGMINE; RIVASTIGMINE; TETRAHYDROFUROBENZOFUROL; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; CARBAMIC ACID DERIVATIVE; CHOLINESTERASE INHIBITOR; DRUG DERIVATIVE; PHYSOSTIGMINE;

ARTICLE; CARBAMOYLATION; CHOLINESTERASE INHIBITION; COMPLEX FORMATION; CONTROLLED STUDY; COVALENT BOND; DRUG BINDING SITE; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENANTIOMER; ENZYME ACTIVE SITE; HYDROPHOBICITY; MICHAELIS CONSTANT; PRIORITY JOURNAL; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; GENETICS; HUMAN; KINETICS; METABOLISM; MUTATION; PROTEIN BINDING;

ACETYLCHOLINESTERASE; BINDING SITES; CATALYSIS; CHOLINESTERASE INHIBITORS; HUMANS; HYDROPHOBICITY; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTATION; PHENYLCARBAMATES; PHYSOSTIGMINE; PROTEIN BINDING; PYRIDOSTIGMINE BROMIDE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 58249088265     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081276     Document Type: Article

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