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Incorporation of Tellurocysteine into Glutathione Transferase Generates High Glutathione Peroxidase Efficiency
Author(s) -
Liu Xiaoman,
Silks Louis A.,
Liu Cuiping,
OllivaultShiflett Morgane,
Huang Xin,
Li Jing,
Luo Guimin,
Hou YaMing,
Liu Junqiu,
Shen Jiacong
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200805365
Subject(s) - gpx3 , gpx6 , glutathione , gpx1 , peroxidase , chemistry , gpx4 , glutathione peroxidase , biochemistry , glutathione reductase , glutathione transferase , enzyme , glutathione s transferase , transferase , residue (chemistry)
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.