Structure and dynamics of serine hydrolase-organophosphate adducts.
The structural profile for the interactions between serine proteases and organophosphorus (OP) compounds can be deduced from recent NMR and X-ray crystallographic data. Using the rationale proposed for serine proteases, dynamic data on the inhibition of acetylcholinesterase by OP compounds is also consistent with structural constraints and an impairment of the proton switch mechanism during phosphorylation.
Kovach
I M
IM
Center for Biomedical Research, University of Kansas, Lawrence 66045.
D000110:Acetylcholinesterase / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000378:metabolism / Q000494:pharmacology; D008962:Models, Theoretical; D009943:Organophosphorus Compounds / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors
D002800:Cholinesterase Inhibitors; D009943:Organophosphorus Compounds; D015842:Serine Proteinase Inhibitors; D000110:Acetylcholinesterase; D012697:Serine Endopeptidases