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Incorporation of Tellurocysteine into Glutathione Transferase Generates High Glutathione Peroxidase Efficiency |
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| Authors: | Xiaoman Liu Louis A Silks Prof Dr Cuiping Liu Dr Morgane Ollivault‐Shiflett Xin Huang Jing Li Dr Guimin Luo Prof Dr Ya‐Ming Hou Prof Dr Junqiu Liu Prof Dr Jiacong Shen Prof |
| Institution: | 1. State Key Laboratory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Road, Changchun 130012 (China), Fax: (+86)?431‐8519‐3421;2. Los Alamos National Laboratory, The National Stable Isotope Resource, Bioscience Division, Los Alamos, MS E529, NM 87545 (USA);3. Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107 (USA) |
| 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.  |
| Keywords: | enzyme models glutathione peroxidase protein design tellurium tellurocysteine |