Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.

Protein engineering, design & selection : PEDS - 1 Jan 2011

Briseño-Roa Luis, Oliynyk Zoryana, Timperley Christopher M, Griffiths Andrew D, Fersht Alan R

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Insecticides
Share to Models, Molecular
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Pseudomonas

Source

Identifiers

PMID: 20650962
DOI: 10.1093/protein/gzq046

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20650962-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.PMID 20650962Read ↗

Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents.Semantic proximity Read ↗

Phosphotriesterase variants with high methylphosphonatase activity and strong negative trade-off against phosphotriesters.Semantic proximity Read ↗

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase.Semantic proximity Read ↗

Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Semantic proximity Read ↗

Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase.Semantic proximity Read ↗

A catalytic bioscavenger with improved stability and reduced susceptibility to oxidation for treatment of acute poisoning with neurotoxic organophosphorus compounds.Semantic proximity Read ↗

Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro.Semantic proximity Read ↗

Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling.Semantic proximity Read ↗

Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR.Semantic proximity Read ↗

Evolution in the amidohydrolase superfamily: substrate-assisted gain of function in the E183K mutant of a phosphotriesterase-like metal-carboxylesterase.Semantic proximity Read ↗

Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides.Semantic proximity Read ↗

High-throughput screening of enzyme libraries: thiolactonases evolved by fluorescence-activated sorting of single cells in emulsion compartments.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.