Phosphotriesterase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
The <scene name='48/489268/Cv/3'>reaction product of PTE is located in the binuclear metal center</scene><ref>PMID:18702530</ref>.Water molecules shown as red spheres. | The <scene name='48/489268/Cv/3'>reaction product of PTE is located in the binuclear metal center</scene><ref>PMID:18702530</ref>.Water molecules shown as red spheres. | ||
| - | Phosphotriesterases have been extensively studied in order to increase their catalytic efficiency by directed evolution and structure based design<ref>PMID:12505981</ref> <ref>PMID: | + | Phosphotriesterases have been extensively studied in order to increase their catalytic efficiency by directed evolution and structure based design<ref>PMID:12505981</ref><ref>PMID:15790580</ref>. |
Revision as of 10:19, 21 August 2018
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3D structures of phosphotriesterase
Updated on 21-August-2018
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
