Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-02

AUTHORS

G Fischer, B Wittmann-Liebold, K Lang, T Kiefhaber, F X Schmid

ABSTRACT

The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was recently discovered in mammalian tissues and purified from porcine kidney. It catalyses the slow cis-trans isomerization of proline peptide (Xaa-Pro) bonds in oligopeptides and accelerates slow, rate-limiting steps in the folding of several proteins. Here, we report the N-terminal sequence of PPIase together with further chemical and enzymatic properties. The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A (CsA). Cyclophilin is thought to be linked to the immunosuppressive action of CsA. The first 38 amino-acid residues of porcine PPIase and of bovine cyclophilin are identical and the two proteins both have a relative molecular mass of about 17,000 (ref. 7). The catalysis of prolyl isomerization in oligopeptides and of protein folding by PPIase are strongly inhibited in the presence of low levels of CsA. The activities of both PPIase and cyclophilin depend on a single sulphydryl group. At present it is unknown whether the inhibition of prolyl isomerase activity is related with the immunosuppressive action of CsA. More... »

PAGES

476-478

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/337476a0

DOI

http://dx.doi.org/10.1038/337476a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052387479

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2492638


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