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- W155460915 abstract "Platelet-activating factor acetylhydrolase (PAFAH) offers a unique platform on which to engineer a catalytic bioscavenger for organophosphorus compounds (OP). Liposome-associated enzymes, like PAFAH and PON1, circulate within the plasma and interact with OPs before cholinergic disruption. Wild type PAFAH and butyrylcholinesterase (BuChE) were tested for their ability to interact with the OPs tabun (GA), sarin (GB), and soman (GD). BuChE could be completely inhibited with 10 uM of each OP while PAFAH was resistant, and maintained at least 55% of original activity. We investigated W298, F322 and L153 within human PAFAH as sites for a secondary nucleophile to improve reactivation of the OP-inhibited enzyme. Mutants screened were less reactive than wild type to the soluble substrates p-nitrophenyl butyrate (PNPB) and 2-thio PAF. We tested mutants against VX, VR, V2 (an analog of VX), and echothiophate, but found no appreciable catalytic power against these OPs. We mutated residue Q352 to G, N, and W to determine its contribution to binding soluble substrates. For the smaller substrate PNPB, all mutants had higher KMs, but catalytic efficiencies were similar to wild type. For 2-thio PAF, Q352N had low activity, whereas Q352W increased the catalytic efficiency by 20-fold over Q352G and 80-fold over wild type by reducing KM. Spontaneous reactivation rates with a variety of OPs will be discussed." @default.
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- W155460915 date "2010-04-01" @default.
- W155460915 modified "2023-09-27" @default.
- W155460915 title "Engineering Platelet‐Activating Factor Acetylhydrolase as a Catalytic Bioscavenger for Organophosphorus Compounds" @default.
- W155460915 doi "https://doi.org/10.1096/fasebj.24.1_supplement.835.8" @default.
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