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

Mutant of Bungarus fasciatus acetylcholinesterase with low affinity and low hydrolase activity toward organophosphorus esters.

Biochimica et biophysica acta - 1 Sept 2006

Poyot Thomas, Nachon Florian, Froment Marie-Thérèse, Loiodice Mélanie, Wieseler Stacy, Schopfer Lawrence M, Lockridge Oksana, Masson Patrick

Abstract excerpt

Enzymes hydrolysing highly toxic organophosphate esters (OPs) are promising alternatives to pharmacological countermeasures against OPs poisoning. Bungarus fasciatus acetylcholinesterase (BfAChE) was engineered to acquire organophosphate hydrolase (OPase) activity by reproducing the features of the human butyrylcholinesterase G117H mutant, the first mutant designed to hydrolyse OPs. The modification consisted of...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcholinesterase
Share to Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Organophosphorus Compounds

Source

Identifiers

PMID: 16962835
DOI: 10.1016/j.bbapap.2006.07.008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutant of Bungarus fasciatus acetylcholinesterase with low affinity and low hydrolase activity toward organophosphorus esters.PMID 16962835Read ↗

Identification of human butyrylcholinesterase organophosphate-resistant variants through a novel mammalian enzyme functional screen.Semantic proximity Read ↗

Organophosphate hydrolases as catalytic bioscavengers of organophosphorus nerve agents.Semantic proximity Read ↗

A rationally designed mutant of plasma platelet-activating factor acetylhydrolase hydrolyzes the organophosphorus nerve agent soman.Semantic proximity Read ↗

Investigating the structural influence of surface mutations on acetylcholinesterase inhibition by organophosphorus compounds and oxime reactivation.Semantic proximity Read ↗

Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure.Semantic proximity Read ↗

Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance.Semantic proximity Read ↗

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

Similar Active Sites and Mechanisms Do Not Lead to Cross-Promiscuity in Organophosphate Hydrolysis: Implications for Biotherapeutic Engineering.Semantic proximity Read ↗

Conformational variability of organophosphorus hydrolase upon soman and paraoxon binding.Semantic proximity Read ↗

Successive organophosphate inhibition and oxime reactivation reveals distinct responses of recombinant human cholinesterase variants.Semantic proximity Read ↗

Computational Design of Phosphotriesterase Improves V-Agent Degradation Efficiency.Semantic proximity Read ↗

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