Artificial selenoenzymes: designed and redesigned.
Enzymes, highly evolved machinery developed by nature, catalyse reactions with formidable efficiency and specificity under mild conditions. Considerable efforts have been devoted for several decades on the development of enzyme-like catalysts with tailored properties by rationally manipulating natural and artificially synthesized host molecules. One of the great challenges is to design artificial systems with catalytic efficiencies and specificities rivalling natural components. Although most of the designed artificial enzymes present mild rate promotion, the high efficiency and specificity rivalling natural ones by artificially designed system appears. In this tutorial review, we recount the methods and strategies of design and redesign of artificial selenoenzymes on synthesized and natural hosts, with emphasis on construction of the active sites of antioxidative glutathione peroxidase (GPx) by the concept of synergy between recognition and catalysis (66 references).
State Key Laboratory for Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, P. R. China.
Xin
X
Huang
Xiaoman
X
Liu
Quan
Q
Luo
Junqiu
J
Liu
Jiacong
J
Shen
D055162:Biocatalysis; D020134:Catalytic Domain; D003505:Cyclodextrins / Q000737:chemistry; D050091:Dendrimers / Q000737:chemistry; D005979:Glutathione Peroxidase / Q000737:chemistry* / Q000378:metabolism; D036103:Nanotechnology; D011108:Polymers / Q000737:chemistry; D015202:Protein Engineering; D017279:Selenocysteine / Q000737:chemistry
D003505:Cyclodextrins; D050091:Dendrimers; D011108:Polymers; D017279:Selenocysteine; D005979:Glutathione Peroxidase