at Google ScholarTitle 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
(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 > 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: | 18 May 2015 10:02 |
| Last Modified: | 28 Feb 2023 13:31 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/13533 |