Phosphotriesterase

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Revision as of 23:04, 14 January 2018

spinqualitylabelsall models Phosphotriesterase dimer complex with reaction product ethyl phosphate and Co+2 ion (pink), 3cak Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phosphotriesterase or aryldialkylphosphatase (PTE) catalyzes the conversion of aryl dialkyl phosphate to dialkyl phosphate and aryl alcohol[1]. For more details see SsoPox: a natural lactonase with promiscuous phosphotriesterase activities. Relevance PTE has no known natural substrate but has potential in detoxification of organophosphates poisons lethal effects. PTE can detoxify the insecticide paraoxon and the chemical warfare agent sarin[2]. Structural highlights The [3].Water molecules shown as red spheres.

3D structures of phosphotriesterase

Updated on 14-January-2018

References

1. ↑ Roodveldt C, Tawfik DS. Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state. Protein Eng Des Sel. 2005 Jan;18(1):51-8. PMID:15790580 doi:http://dx.doi.org/10.1093/protein/gzi005
2. ↑ Bigley AN, Mabanglo MF, Harvey SP, Raushel FM. Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR. Biochemistry. 2015 Aug 25. PMID:26274608 doi:http://dx.doi.org/10.1021/acs.biochem.5b00629
3. ↑ Kim J, Tsai PC, Chen SL, Himo F, Almo SC, Raushel FM. Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase. Biochemistry. 2008 Sep 9;47(36):9497-504. Epub 2008 Aug 15. PMID:18702530 doi:10.1021/bi800971v