2009Angewandte Chemie International EditionRequires access

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

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Abstract

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.

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What this paper is about

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.

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Available abstract

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.

Key concepts: GPX3, GPX6, Glutathione, GPX1, Peroxidase, Chemistry, GPX4, Glutathione peroxidase

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