FEBS Lett. 1991 Jun 17;284(1):79-81.

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

Hübner D, Drakenberg T, Forsén S, Fischer G.

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Department of Biochemistry, Martin-Luther-University, Halle, Germany.

Abstract

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.

PMID:: 2060630; [PubMed - indexed for MEDLINE]

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Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy. [Biochemistry. 1995]
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Cited by 1 PubMed Central article

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