Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.

Protein Engineering, Design & Selection : PEDS
Luis Briseño-RoaAlan R Fersht

Abstract

The bacterial phosphotriesterase (PTE) catalyses the hydrolysis of the man-made pesticide paraoxon with a diffusion-limited efficiency. Here we describe the selection and characterisation of PTE variant SS0.2 that possesses the highest paraoxonase turnover number so far described (k(cat) = 31,000 s⁻¹). The PTE-SS0.2 was selected from a library of binding-site mutants using a novel screening method that combines partial lysis of bacterial colonies and fluorogenic probes.

References

Nov 19, 1974·Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character·A R Fersht
Sep 1, 1972·The Biochemical Journal·S J PutmanJ R Knowles
Dec 31, 2002·The EMBO Journal·Andrew D Griffiths, Dan S Tawfik
Dec 8, 2009·Proceedings of the National Academy of Sciences of the United States of America·C J JacksonD L Ollis

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Citations

Sep 18, 2013·ACS Chemical Biology·Izhack ChernyDan S Tawfik
Aug 18, 2017·Molecular BioSystems·Andrew J OlsenJin Kim Montclare
Oct 27, 2018·Journal of Pesticide Science·Karla Alejo-GonzálezRafael Vazquez-Duhalt
Aug 8, 2021·International Journal of Molecular Sciences·Pauline JacquetDavid Daudé

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