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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hübner D,Drakenberg T,Forsén S,Fischer Gdoi
10.1016/0014-5793(91)80766-vsubject
Has Abstractpub_date
1991-06-17 00:00:00pages
79-81issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(91)80766-Vjournal_volume
284pub_type
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