Artificial selenoenzymes: Designed and redesigned

被引:165
作者
Huang, Xin [1 ]
Liu, Xiaoman [1 ]
Luo, Quan [1 ]
Liu, Junqiu [1 ]
Shen, Jiacong [1 ]
机构
[1] Jilin Univ, Coll Chem, State Key Lab Supramol Struct & Mat, Changchun 130012, Peoples R China
关键词
GLUTATHIONE-PEROXIDASE ACTIVITY; HIGH CATALYTIC EFFICIENCY; SYNTHETIC ORGANOSELENIUM COMPOUNDS; SELENIUM-CONTAINING PROTEIN; ACTIVE-SITE; BETA-CYCLODEXTRIN; CHEMICAL MUTATION; ANTIOXIDANT ACTIVITY; KINETIC MECHANISM; CRYSTAL-STRUCTURE;
D O I
10.1039/c0cs00046a
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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).
引用
收藏
页码:1171 / 1184
页数:14
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