Abstract
The cytosolic peptidyl‐prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One‐ and two‐dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.
Original language | English |
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Pages (from-to) | 198-203 |
Journal | FEBS Letters |
Volume | 323 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1993 |
MoE publication type | A1 Journal article-refereed |