The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

D. Hubner, Torbjörn Drakenberg, M. Wikström, Sture Forsen, H. Bang, G. Fischer

Research output: Contribution to journalArticleScientificpeer-review

42 Citations (Scopus)

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 languageEnglish
Pages (from-to)198 - 203
Number of pages6
JournalFEBS Letters
Volume323
Issue number3
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

Fingerprint Dive into the research topics of 'The <i>cis</i>/<i>trans</i> interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin'. Together they form a unique fingerprint.

  • Cite this

    Hubner, D., Drakenberg, T., Wikström, M., Forsen, S., Bang, H., & Fischer, G. (1993). The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS Letters, 323(3), 198 - 203. https://doi.org/10.1016/0014-5793(93)81338-Z