Structure and Dynamics of Serine Hydrolase-Organophosphate Adducts
- 1 January 1988
- journal article
- research article
- Published by Taylor & Francis in Journal of Enzyme Inhibition
- Vol. 2 (3) , 199-208
- https://doi.org/10.3109/14756368809040726
Abstract
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.Keywords
This publication has 23 references indexed in Scilit:
- Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesChemical Reviews, 1987
- Nitrogen-15 NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanismBiochemistry, 1986
- Catalytic recruitment in the inactivation of serine proteases by phosphonate esters. Recruitment of acid-base catalysisJournal of the American Chemical Society, 1986
- Stereochemical aspects of cholinesterase catalysisBioorganic Chemistry, 1984
- Inhibition of acetylcholinesterase from different species by organophosphorus compounds, carbamates and methylsulphonylfluorideGeneral Pharmacology: The Vascular System, 1977
- Reactivation and aging of diphenyl phosphoryl acetylcholinesteraseBiochimica et Biophysica Acta (BBA) - Enzymology, 1975
- Equilibrium constants for the phosphorylation of acetylcholinesterase by some diethyl phosphorothiolates and phosphatesBiochemistry, 1974
- The inhibition of acetylcholinesterase by organophosphorus compounds containing a PCl bondBiochimica et Biophysica Acta (BBA) - Enzymology, 1974
- Mechanisms of Nucleophilic Substitution in Phosphate EstersChemical Reviews, 1964
- Cholinesterases and Anticholinesterase AgentsPublished by Springer Nature ,1963