Incorporation of tellurocysteine into glutathione transferase generates high glutathione peroxidase efficiency.
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.
Liu
Xiaoman
X
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Road, Changchun 130012, China.
Silks
Louis A
LA
Liu
Cuiping
C
Ollivault-Shiflett
Morgane
M
Huang
Xin
X
Li
Jing
J
Luo
Guimin
G
Hou
Ya-Ming
YM
Liu
Junqiu
J
Shen
Jiacong
J
D002384:Catalysis; D003545:Cysteine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D005979:Glutathione Peroxidase / Q000378:metabolism*; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000737:chemistry; D010084:Oxidation-Reduction
C540155:tellurocysteine; D006861:Hydrogen Peroxide; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D003545:Cysteine