| Literature DB >> 8500610 |
D Kern1, T Drakenberg, M Wikström, S Forsén, H Bang, G Fischer.
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.Entities:
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Year: 1993 PMID: 8500610 DOI: 10.1016/0014-5793(93)81338-z
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124