The mode of action of peptidyl prolyl cis/trans isomerases in vivo:: binding vs. catalysis

被引：112

作者：

Fischer, G ^{[1
]}

Tradler, T ^{[1
]}

Zarnt, T ^{[1
]}

机构：

[1] Max Planck Gesell, Res Unit Enzymol Prot Folding, D-06120 Halle, Germany

来源：

FEBS LETTERS | 1998年 / 426卷 / 01期

关键词：

D O I：

10.1016/S0014-5793(98)00242-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Polypeptides often display proline-mediated conformational substates that are prone to isomer-specific recognition and function. Both possibilities can be of biological significance. Distinct families of peptidyl prolyl cis/trans isomerases (PPIases) evolved proved to be highly specific for proline moieties arranged in a special contest of subsites, Structural and chemical features of molecules specifically bound to the active site of PPIases served to improve catalysis of prolyl isomerization rather than ground state binding. For example, results inferred from receptor Ser/Thr or Tyr phosphorylation in the presence of site-directed FKBP12 mutant proteins provided evidence for the crucial role of the enzymatic activity in downregulating function of FKBP12. (C) 1998 Federation of European Biochemical Societies.

引用

页码：17 / 20

页数：4

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