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

Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase.

Bioresource technology - 1 Dec 2010

Merone Luigia, Mandrich Luigi, Porzio Elena, Rossi Mosé, Müller Susanne, Reiter Georg, Worek Franz, Manco Giuseppe

Abstract excerpt

The thermostable Phosphotriesterase-Like Lactonase from Sulfolobus solfataricus (SsoPox) hydrolyzes lactones and, at a lower rate, neurotoxic organophosphorus compounds. The persistent demand of detoxification tools in the field of agricultural wastes and restoring of conditions after terrorist acts prompted us to exploit SsoPox as a "starter" to evolve its ancillary nerve agents hydrolytic capability. A directed...

Read the complete abstract on PubMed

Topics

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

Share to Biodegradation, Environmental
Share to Carboxylic Ester Hydrolases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

Share to Enzyme Assays

Share to Enzyme Stability

Share to Hydrolysis

Share to Sodium Dodecyl Sulfate

Share to Sulfolobus solfataricus

Source

Identifiers

PMID: 20667718
DOI: 10.1016/j.biortech.2010.06.102

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase.PMID 20667718Read ↗

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

Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.Semantic proximity Read ↗

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

Innate and adaptive immune responses to the injection of hybrid camouflaging erythrocyte Saccharolobus solfataticus-phosphotriesterase mutant-loaded nanoreactors to mice.Semantic proximity Read ↗

Biochemical characterization and mutational improvement of a thermophilic esterase from Sulfolobus solfataricus P2.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 ↗

Binuclear Metallohydrolases: Complex Mechanistic Strategies for a Simple Chemical ReactionSemantic 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 ↗

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

Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.Semantic proximity Read ↗

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