title: Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.
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.
authors.affiliation: MRC Centre for Protein Engineering, Hills Road, Cambridge CB20QH, UK. briseno@biologie.ens.fr
authors.forename: Luis
authors.initials: L
authors.lastname: Briseño-Roa
authors.forename: Zoryana
authors.initials: Z
authors.lastname: Oliynyk
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Timperley
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Griffiths
authors.forename: Alan R
authors.initials: AR
authors.lastname: Fersht
mesh_terms: D007306:Insecticides / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D010261:Paraoxon / Q000378:metabolism*; D044345:Phosphoric Triester Hydrolases / Q000235:genetics* / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics
chemical_list: D007306:Insecticides; D044345:Phosphoric Triester Hydrolases; D010261:Paraoxon