Peptidyl‐prolyl cis‐trans isomerase activity as studied by dynamic proton NMR spectroscopy

FEBS Letters

Drakenberg, Torbjörn²  Hübner, Dorothee¹  Fischer, Gunter²  Forsén, Sture² 

[1] Department of Biochemistry, Martin-Luther-University, Halle-Wittenberg, Weinbergweg 16, D-4050 Halle, Germany;Department of Physical Chemistry 2, Chemical Center, University of Lund, POB 124, S-221 00 Lund, Sweden

关键词: Peptidyl-prolyl cis-trans isomerase;    Cyclophilin;    Cyclosporin A;    Prolin cis-trans isomerism;    1H dynamic NMR;    Bandshape analysis;   

DOI  :  10.1016/0014-5793(91)80766-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recently the identity of the peptidyl-prolyl cis-trans isomerase (PPIase), which accelerates the cis/trans isomerization of prolyl peptide bonds and cyclophilin, the binding protein for the immunosuppressive drug Cyclosporin A (CsA), was discovered. The PPIase catalysis toward the substrate Suc-Ala-Phe-Pro-Phe-pNA has been studied by ¹H NMR spectroscopy. Using the bandshape analysis technique the rate of interconversion between the cis and trans isomers of the substrate could be measured in the presence of PPIase and under equilibrium conditions. The acceleration is inhibited by equimolar amounts of CsA. The results provide evidence that the PPIase catalysis is more complex than a simple exchange between two states.

【 授权许可】

Unknown