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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.  Ph1 prol (PH0974) has previously been isolated and characterized from  Pyrococcus horikoshii  and was shown to have higher catalytic activity over a broader pH range, higher affinity for metal, and increased thermostability compared to  P. furiosus  prolidase,  Pf prol (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 mutated  Ph1 prol enzymes were prepared. Four  Ph1 prol mutants (A195T/G306S-, Y301C/K342N-, E127G/E252D-, and E36V- Ph1 prol) 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 type  Pyrococcus  prolidases.

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Improving the Catalytic Activity of Hyperthermophilic<i>Pyrococcus horikoshii</i>Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures

Improving the Catalytic Activity of HyperthermophilicPyrococcus horikoshiiProlidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures