Accession Number : ADA553625


Title :   Improving the Catalytic Activity of Hyperthermophilic Pyrococcus horikoshii Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures


Descriptive Note : Research article


Corporate Author : ARMY EDGEWOOD CHEMICAL BIOLOGICAL CENTER APG MD


Personal Author(s) : Theriot, Casey M ; Semcer, Rebecca L ; Shah, Saumil S ; Grunden, Amy M


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a553625.pdf


Report Date : Jan 2011


Pagination or Media Count : 10


Abstract : 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 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 Ph1prol enzymes were prepared. Four Ph1prolmutants (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 type Pyrococcus prolidases.


Descriptors :   *NERVE AGENTS , CATALYSTS , DETOXIFICATION , ENZYMES , GD AGENT , ORGANIC PHOSPHORUS COMPOUNDS , PH FACTOR , PROTEINS , REPRINTS , THERMAL STABILITY


Subject Categories : Chemical, Biological and Radiological Warfare


Distribution Statement : APPROVED FOR PUBLIC RELEASE