Abstract
The stereoselectivity of acetylcholinesterase (EC 3.1.1.7) and butyrylcholinesterase (EC 3.1.1.8) was studied in the interaction with enantiomers of quinuclidin-3-yl acetates as substrates as well as in the reversible inhibition of the enzymes by enantiomers of quinuclidin-3-ol derivatives. For that purpose (R)- and (S)-alcohols and their acetates as well as their quaternary N-methyl and N-benzyl derivatives were prepared and characterized.
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