ArticlePhilosophical transactions. Series A, Mathematical, physical, and engineering sciences2016
Probing the mechanisms for the selectivity and promiscuity of methyl parathion hydrolase.
Article in Philosophical transactions. Series A, Mathematical, physical, and engineering sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Single-molecule kinetic exploration of functional sub-states in an evolving phosphotriesterase.Nature communications · 2026Article
- A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.Chembiochem : a European journal of chemical biology · 2025Article
- Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.JACS Au · 2024Article
- Coupling Peptide-Based Encapsulation of Enzymes with Bacteria for Paraoxon Bioremediation.ACS applied materials & interfaces · 2024Article
- Why Monoamine Oxidase B Preferably MetabolizesInternational journal of molecular sciences · 2022Article
- The adaptive landscape of a metallo-enzyme is shaped by environment-dependent epistasis.Nature communications · 2021Article
- Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase.Computational and structural biotechnology journal · 2021Article
- Higher-order epistasis shapes the fitness landscape of a xenobiotic-degrading enzyme.Nature chemical biology · 2019Article
- Novel mutation inJournal of genetics · 2019Article
- Similar Active Sites and Mechanisms Do Not Lead to Cross-Promiscuity in Organophosphate Hydrolysis: Implications for Biotherapeutic Engineering.Journal of the American Chemical Society · 2017Article
- Extending the Nonbonded Cationic Dummy Model to Account for Ion-Induced Dipole Interactions.The journal of physical chemistry letters · 2017Article
- Bridging the gaps at the physics-chemistry-biology interface.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diverse organophosphate hydrolases have convergently evolved the ability to hydrolyse man-made organophosphates. Thus, these enzymes are attractive model systems for studying the factors shaping enzyme functional evolution. Methyl parathion hydrolase (MPH) is an enzyme from the metallo-β-lactamase superfamily, which hydrolyses a wide range of organophosphate, aryl ester and lactone substrates. In addition, MPH demonstrates metal-ion-dependent selectivity patterns. The origins of this remain unclear, but are linked to open questions about the more general role of metal ions in functional evolution and divergence within enzyme superfamilies. Here, we present detailed mechanistic studies of the paraoxonase and arylesterase activities of MPH complexed with five different transition metal ions, and demonstrate that the hydrolysis reactions proceed via similar pathways and transition states. However, while it is possible to discern a clear structural origin for the selectivity between different substrates, the selectivity between different metal ions appears to lie instead in the distinct electrostatic properties of the metal ions themselves, which causes subtle changes in transition state geometries and metal-metal distances at the transition state rather than significant structural changes in the active site. While subtle, these differences can be significant for shaping the metal-ion-dependent activity patterns observed for this enzyme.This article is part of the themed issue 'Multiscale modelling at the physics-chemistry-biology interface'.
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