Phosphotriesterase

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Phosphotriesterase dimer complex with reaction product ethyl phosphate and Co+2 ion (pink), 3cak

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3D structures of phosphotriesterase

Updated on 21-August-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
  4. Griffiths AD, Tawfik DS. Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization. EMBO J. 2003 Jan 2;22(1):24-35. doi: 10.1093/emboj/cdg014. PMID:12505981 doi:http://dx.doi.org/10.1093/emboj/cdg014
  5. 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

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Michal Harel, Joel L. Sussman, Alexander Berchansky

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