ArticleProtein science : a publication of the Protein Society2013
Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Tetranectin and Paraoxonase-1 as Markers of Heart Failure.Medicina (Kaunas, Lithuania) · 2026Review
- Challenges and advances in the development of antidotes against A-series nerve agents.Archives of toxicology · 2026Review
- Novel Self-Cleaving Affinity Purification Method for Cellular Membrane-Associated Recombinant Paraoxonase-1 (rePON1) Enzyme.The protein journal · 2025Article
- Human Paraoxonase 1: From Bloodstream Enzyme to Disease Fighter & Therapeutic Intervention.Current protein & peptide science · 2025Review
- 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
- Enzymatic Bioremediation of Organophosphate Compounds-Progress and Remaining Challenges.Frontiers in bioengineering and biotechnology · 2019Review
- Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead.The protein journal · 2016Review
- Toward Understanding the Catalytic Mechanism of Human Paraoxonase 1: Site-Specific Mutagenesis at Position 192.PloS one · 2016Article
- Human paraoxonase 1 as a pharmacologic agent: limitations and perspectives.TheScientificWorldJournal · 2014Review
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Abstract
Human paraoxonase 1 (h-PON1) hydrolyzes variety of substrates and the hydrolytic activities of enzyme can be broadly grouped into three categories; arylesterase, phosphotriesterase, and lactonase. Current models of the catalytic mechanism of h-PON1 suggest that catalytic residues H115 and H134 mediate the lactonase and arylesterase activities of the enzyme. H-PON1 is a strong candidate for the development of catalytic bioscavenger for organophosphate poisoning in humans. Recently, Gupta et al. (Nat. Chem. Biol. 2011. 7, 120) identified amino acid substitutions that significantly increased the activity of chimeric-PON1 variant (4E9) against some organophosphate nerve agents. In this study we have examined the effect of these (L69G/S111T/H115W/H134R/R192K/F222S/T332S) and other substitutions (H115W/H134R and H115W/H134R/R192K) on the hydrolytic activities of recombinant h-PON1 (rh-PON1) variants. Our results show that the substitutions resulted in a significant increase in the organophosphatase activity of all the three variants of rh-PON1 enzyme while had a variable effect on the lactonase/arylesterase activities. The results suggest that H residues at positions 115 and 134 are not always needed for the lactonase/arylesterase activities of h-PON1 and force a reconsideration of the current model(s) of the catalytic mechanism of h-PON1.
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