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Incorporation of tellurocysteine into glutathione transferase generates high glutathione peroxidase efficiency

  • Xiaoman Liu*
  • , Louis A. Silks
  • , Cuiping Liu
  • , Morgane Ollivault-Shiflett
  • , Xin Huang
  • , Jing Li
  • , Guimin Luo
  • , Ya Ming Hou
  • , Junqiu Liu
  • , Jiacong Shen
  • *Corresponding author for this work
  • Jilin University
  • Los Alamos National Laboratory
  • Thomas Jefferson University

Research output: Contribution to journalArticlepeer-review

Abstract

(Chemical Equation Presented) A rival to native peroxidase! An existing binding site for glutathione was combined with the catalytic residue tellurocysteine by using an auxotrophic expression system to create an engineered enzyme that functions as a glutathione peroxidase from the scaffold of a glutathione transferase (see picture). The catalytic activity of the telluroenzyme in the reduction of hydroperoxides by glutathione is comparable to that of native glutathione peroxidase.

Original languageEnglish
Pages (from-to)2020-2023
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number11
DOIs
StatePublished - 2 Mar 2009
Externally publishedYes

Keywords

  • Enzyme models
  • Glutathione peroxidase
  • Protein design
  • Tellurium
  • Tellurocysteine

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