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• W2011154552 abstract "Irreversible inhibition of butrylcholinesterase by soman was studied in the presence of the substrate (o-nittophenyl butyrate). Inhibition was found of the competitive complexing type. Study at different temperatures and pressures showed that the behavior of the enzyme differs from that of the inhibitior-free enzyme. In the absence of inhibitor, enzyme kinetics displayed a non-linear temperature dependence with a break at 21°C. In the presence of a non-inhibitor, structural analog of soman (pinacolyl dimethylphosphinate and methyl dimethylphosphinate) the Arrchenius plot break is slightly shifted (18°c). On the other hand, in the presence of soman this break is abolished. The pressure-dependence of the substrate hydrolysis revealed also differences between the native enzyme and the enzyme in the presence of soman: the sign and magnitude of the apparent activation volume (ΔV≠) were different for the two reactions. Beyond 300 bar, in the presence of soman, a plateau (ΔV≠ approx. 0) was observed over a large pressure range depending on temperature. Such a behavior with respect to temperature and pressure can reflect a soman-induced enzyme conformational state. Thus, temperature and pressure perturbations of the kinetics allows to complete the inhibition scheme of butyrylcholinesterase by soman. Our data suggest that upon soman binding, the enzymes undergoes a long-lived soman-induced-fit conformational change preceeding the phosphonylation step. However, an alternative hypothesis according to which the enzyme pocesses a secondary soman-binding site cannot be ruled out." @default.
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• W2011154552 date "1992-10-01" @default.
• W2011154552 modified "2023-10-18" @default.
• W2011154552 title "Soman inhibition of butyrylcholinesterase in the presence of substrate: pressure and temperature perturbations" @default.
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• W2011154552 doi "https://doi.org/10.1016/0167-4838(92)90059-m" @default.
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