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Activation of Hydrogen Peroxide to Peroxytetradecanoic Acid Is Responsible for Potent Inhibition of Protein Tyrosine Phosphatase CD45

Authors
Journal
PLoS ONE
1932-6203
Publisher
Public Library of Science
Publication Date
Volume
7
Issue
12
Identifiers
DOI: 10.1371/journal.pone.0052495
Keywords
  • Research Article
  • Biology
  • Biochemistry
  • Enzymes
  • Enzyme Classes
  • Hydrolases
  • Oxidoreductases
  • Biomacromolecule-Ligand Interactions
  • Chemical Biology
  • Biophysics
  • Molecular Cell Biology
  • Signal Transduction
  • Mechanisms Of Signal Transduction
  • Chemistry
  • Medicinal Chemistry
Disciplines
  • Biology
  • Computer Science

Abstract

Hydrogen peroxide induces oxidation and consequently inactivation of many protein tyrosine phosphatases. It was found that hydrogen peroxide, in the presence of carboxylic acids, was efficiently activated to form even more potent oxidant - peroxy acid. We have found that peroxytetradecanoic acid decreases the enzymatic activity of CD45 phosphatase significantly more than hydrogen peroxide. Our molecular docking computational analysis suggests that peroxytetradecanoic acid has a higher binding affinity to the catalytic center of CD45 than hydrogen peroxide.

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