PubMed · 5747662
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M J De Luna Infante. 1968. [Acholest "test"].. https://pubmed.ncbi.nlm.nih.gov/5747662/
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Pivaloyl-choline iodide 1 interactions with acetylcholinesterase (AChE) have been studied by theoretical and enzymatic methods. An integrated computational approach has clearly shown a substrate rather than inhibitory profile for 1. Enzymatic experiments have also supported the same theoretical conclusion indicating that AChE was able to hydrolyze 1 to choline.
Highly efficient acetylcholinesterase (AChE) and serotonin transporter (SERT) dual inhibitors, (S)-4 and (R)-13 were designed and synthesized on the basis of the hypothetical model of AChE active site. Both compounds showed potent inhibitory activities against AChE and SERT. [structure: see text]
The active site structures of hydrolytic enzymes representing five different protein folds were compared. They contain a strand-helix motif with an active site nucleophile occupying a less favourable region in the Ramachandran plot, as previously described for the alpha/beta-hydrolases. Comparison of the different structures enabled a characterisation of the common denominator and suggests an explanation for the unusual Ramachandran values. According to this, the Ramachandran values reflect the orientation of one of the backbone amino group that stabilises the oxyanion intermediate of catalysis.