Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.

Journal of the American Chemical Society - 25 Jan 2017

Blaha-Nelson David, Krüger Dennis M, Szeler Klaudia, Ben-David Moshe, Kamerlin Shina Caroline Lynn

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aryldialkylphosphatase
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Biocatalysis

Share to Hydrolysis

Share to Hydrophobic and Hydrophilic Interactions

Share to Lactones

Share to Molecular Dynamics Simulation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 28026940
DOI: 10.1021/jacs.6b10801
PMCID: PMC5269640

Genes

PON1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.PMID 28026940Read ↗

Towards Understanding the Catalytic Mechanism of Human Paraoxonase 1: Experimental and In Silico Mutagenesis Studies.Semantic proximity Read ↗

Catalytic stimulation by restrained active-site floppiness--the case of high density lipoprotein-bound serum paraoxonase-1.Semantic proximity Read ↗

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

Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Theoretical Studies on Catalysis Mechanisms of Serum Paraoxonase 1 and Phosphotriesterase Diisopropyl Fluorophosphatase Suggest the Alteration of Substrate Preference from Paraoxonase to DFP.Semantic proximity Read ↗

The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases.Semantic proximity Read ↗

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.Semantic proximity Read ↗

Multiscale Simulations Reveal Distal Allosteric Reprogramming of Pocket Dynamics and Dual Hydrolytic Pathways in Engineered Methyl Parathion Hydrolase.Semantic proximity Read ↗

Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Semantic proximity Read ↗

Organophosphate Hydrolysis by a Designed Metalloenzyme: Impact of Mutations Explained.Semantic proximity Read ↗

Molecular Structure of Paraoxonase-1 and Its Modifications in Relation to Enzyme Activity and Biological Functions-A Comprehensive Review.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.