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Catalysis of protein folding by cyclophilins from different species

Title data

Schönbrunner, Erhard Ralf ; Mayer, Sabine ; Tropschug, Maximilian ; Fischer, Gunter ; Takahashi, Nobuhiro ; Schmid, Franz X.:
Catalysis of protein folding by cyclophilins from different species.
In: The Journal of Biological Chemistry. Vol. 266 (1991) Issue 6 . - pp. 3630-3635.
ISSN 1083-351X
DOI: https://doi.org/10.1016/S0021-9258(19)67841-5

Official URL: Volltext

Abstract in another language

Cyclophilins are a class of ubiquitous proteins with yet unknown function. They were originally discovered as the major binding proteins for the immunosuppressant cyclosporin A. The only known catalytic function of these proteins in vitro is the cis/trans isomerization of Xaa-Pro bonds in oligopeptides. This became clear after the discovery that bovine cyclophilin is identical with porcine prolyl isomerase. This enzyme accelerates slow, proline-limited steps in the refolding of several proteins. Here we demonstrate that the cyclophilins from man, pig, Neurospora crassa, Saccharomyces cerevisiae, and Escherichia coli are all active as prolyl isomerases and as catalysts of protein folding. This evolutionary conservation suggests that catalysis of prolyl peptide bond isomerization may be an important function of the cyclophilins. It could be related with de novo protein folding or be involved in regulatory processes. Catalysis of folding is very efficient in the presence of the high cellular concentrations of prolyl isomerase.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 1825312
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professor Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 13 May 2015 06:24
Last Modified: 28 Feb 2023 12:51
URI: https://eref.uni-bayreuth.de/id/eprint/13439