ArticleChemistryOpen2024
Computational Design of Phosphotriesterase Improves V-Agent Degradation Efficiency.
Article in ChemistryOpen, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Computational Design of Phosphotriesterase Improves V-Agent Degradation Efficiency.ChemistryOpen · 2024Article
- Supercharged Phosphotriesterase for improved Paraoxon activity.Protein engineering, design & selection : PEDS · 2024Article
- Improving stereoselectivity of phosphotriesterase (PTE) for kinetic resolution of chiral phosphates.Frontiers in bioengineering and biotechnology · 2024Article
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Authors and funding
17 authors.
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Abstract
Organophosphates (OPs) are a class of neurotoxic acetylcholinesterase inhibitors including widely used pesticides as well as nerve agents such as VX and VR. Current treatment of these toxins relies on reactivating acetylcholinesterase, which remains ineffective. Enzymatic scavengers are of interest for their ability to degrade OPs systemically before they reach their target. Here we describe a library of computationally designed variants of phosphotriesterase (PTE), an enzyme that is known to break down OPs. The mutations G208D, F104A, K77A, A80V, H254G, and I274N broadly improve catalytic efficiency of VX and VR hydrolysis without impacting the structure of the enzyme. The mutation I106 A improves catalysis of VR and L271E abolishes activity, likely due to disruptions of PTE's structure. This study elucidates the importance of these residues and contributes to the design of enzymatic OP scavengers with improved efficiency.
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