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Article

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

Journal of the American Chemical Society - 6 Dec 2017

Purg Miha, Elias Mikael, Kamerlin Shina Caroline Lynn

Abstract excerpt

Organophosphate hydrolases are proficient catalysts of the breakdown of neurotoxic organophosphates and have great potential as both biotherapeutics for treating acute organophosphate toxicity and as bioremediation agents. However, proficient organophosphatases such as serum paraoxonase 1 (PON1) and the organophosphate-hydrolyzing lactonase SsoPox are unable to hydrolyze bulkyorganophosphates with challenging...

Topics

Aryldialkylphosphatase
Catalytic Domain
Humans
Hydrogen-Ion Concentration
Hydrolysis
Mutation
Organophosphates
Phosphoric Triester Hydrolases
Protein Engineering
Static Electricity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 29113434
DOI: 10.1021/jacs.7b09384
PMCID: PMC5724027

Genes

PON1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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