ArticleJournal of the American Chemical Society2017
Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed.
- The Paraoxonase (International journal of molecular sciences · 2025Review
- Calcitriol Induces Paraoxonase 1 Expression in HepG2 Cells: Possible Involvement of VDR-Dependent and Alternative Pathways.International journal of molecular sciences · 2025Article
- Unlocking Lactonase Enzymes as Biocatalysts for the Deracemisation of Chiral γ-Thiolactones.Angewandte Chemie (International ed. in English) · 2025Article
- Systematic pore lipophilization to enhance the efficiency of an amine-based MOF catalyst in the solvent-free Knoevenagel reaction.Beilstein journal of organic chemistry · 2025Article
- Molecular Structure of Paraoxonase-1 and Its Modifications in Relation to Enzyme Activity and Biological Functions-A Comprehensive Review.International journal of molecular sciences · 2024Review
- Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.JACS Au · 2024Article
- Modulatory Effect of Lifestyle-Related, Environmental and Genetic Factors on Paraoxonase-1 Activity: A Review.International journal of environmental research and public health · 2023Review
- Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases.Chemical science · 2022Article
- Article
- Functional enzyme-polymer complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification of key amino acid residues toward improving the catalytic activity and substrate specificity of plant-derived cytochrome P450 monooxygenases CYP716A subfamily enzyme for triterpenoid production inFrontiers in bioengineering and biotechnology · 2022Article
- Human carboxylesterases and fluorescent probes to image their activity in live cells.RSC medicinal chemistry · 2021Review
- Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases.Journal of the American Chemical Society · 2021Article
- Temperature-Dependent Kinetic Isotope Effects in R67 Dihydrofolate Reductase from Path-Integral Simulations.The journal of physical chemistry. B · 2021Article
- From Ru-bda to Ru-bds: a step forward to highly efficient molecular water oxidation electrocatalysts under acidic and neutral conditions.Nature communications · 2021Article
- Ground-State Destabilization by Active-Site Hydrophobicity Controls the Selectivity of a Cofactor-Free Decarboxylase.Journal of the American Chemical Society · 2020Article
- Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase.ACS catalysis · 2020Article
- Selective Delivery of Dicarboxylates to Mitochondria by Conjugation to a Lipophilic Cation via a Cleavable Linker.Molecular pharmaceutics · 2020Article
- Effects ofAntioxidants (Basel, Switzerland) · 2020Article
- Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. Structurally, PON1 is a six-bladed β-propeller with a flexible loop (residues 70-81) covering the active site. This loop contains a functionally critical Tyr at position 71. We have performed detailed experimental and computational analyses of the role of selected Y71 variants in the active site stability and catalytic activity in order to probe the role of Y71 in PON1's lactonase and organophosphatase activities. We demonstrate that the impact of Y71 substitutions on PON1's lactonase activity is minimal, whereas the k
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.