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

Dorothee Kern, Torbjörn Drakenberg, Mats Wikström, Sture Forsén, Holger Bang, Gunter 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
JournalFEBS Letters
Volume323
Issue number3
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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