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Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate

Title data

Scholz, Christian ; Schindler, Thomas ; Dolinski, Kara ; Heitman, Joseph ; Schmid, Franz X.:
Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate.
In: FEBS Letters. Vol. 414 (1 September 1997) Issue 1 . - pp. 69-73.
ISSN 1873-3468
DOI: https://doi.org/10.1016/S0014-5793(97)00979-4

Abstract in another language

The prolyl isomerase activity of cyclophilins is traditionally measured by an assay in which prolyl cis/trans isomerization in a chromogenic tetrapeptide is coupled with its isomer-specific cleavage by chymotrypsin. Two variants of mitochondrial cyclophilin with substitutions in the presumed active site (R73A and H144Q) are inactive in the protease-coupled assay, but show almost wild-type activity in an assay that is based on the catalysis of a proline-limited protein folding reaction. This prolyl isomerase assay is preferable, both because coupling with proteolysis is avoided and because an intact protein instead of a short peptide is used as a substrate. Possibly, some earlier conclusions about the catalytic mechanism and the involvement of the prolyl isomerase activity in the cellular function of immunophilins may need reevaluation.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 9305734
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship 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: 18 May 2015 10:02
Last Modified: 11 Mar 2016 10:43
URI: https://eref.uni-bayreuth.de/id/eprint/13533