@article{theriot_semcer_shah_grunden_2011, title={Improving the Catalytic Activity of Hyperthermophilic Pyrococcus horikoshii Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures}, volume={2011}, ISSN={1472-3646 1472-3654}, url={http://dx.doi.org/10.1155/2011/565127}, DOI={10.1155/2011/565127}, abstractNote={Prolidases hydrolyze Xaa-Pro dipeptides and can also cleave the P-F and P-O bonds found in organophosphorus (OP) compounds, including the nerve agents soman and sarin.Ph1prol (PH0974) has previously been isolated and characterized fromPyrococcus horikoshiiand was shown to have higher catalytic activity over a broader pH range, higher affinity for metal, and increased thermostability compared toP. furiosusprolidase,Pfprol (PF1343). To obtain a better enzyme for OP nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity, randomly mutatedPh1prol enzymes were prepared. FourPh1prol mutants (A195T/G306S-, Y301C/K342N-, E127G/E252D-, and E36V-Ph1prol) were isolated which had greater thermostability and improved activity over a broader range of temperatures against Xaa-Pro dipeptides and OP nerve agents compared to wild typePyrococcusprolidases.}, journal={Archaea}, publisher={Hindawi Limited}, author={Theriot, Casey M. and Semcer, Rebecca L. and Shah, Saumil S. and Grunden, Amy M.}, editor={C.M., B.Semcer and Shah, S.Editors}, year={2011}, pages={1–9} }