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Prolyl isomerases show low sequence specificity toward the residue following the proline

Title data

Schmidpeter, Philipp A. M. ; Jahreis, Günther ; Geitner, Anne-Juliane ; Schmid, Franz X.:
Prolyl isomerases show low sequence specificity toward the residue following the proline.
In: Biochemistry. Vol. 50 (31 May 2011) Issue 21 . - pp. 4796-4803.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi200442q

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Abstract in another language

Prolyl isomerases catalyze the cis/trans isomerization of peptide bonds preceding proline. Previously, we had determined the specificity toward the residue before the proline for cyclophilin-, FKBP-, and parvulin-type prolyl isomerases by using proline-containing oligopeptides and refolding proteins as model substrates. Here, we report the specificities of members of these three prolyl isomerase families for the residue following the proline, again in short peptide and in refolding protein chains. Human cyclophilin 18 and parvulin 10 from Escherichia coli show high activity, but low specificity, with respect to the residue following the proline. Human FKBP12 prefers hydrophobic residues at this position in the peptide assays and shows a very low activity in the protein folding assays. This activity was strongly improved, and the sequence specificity was virtually eliminated after the insertion of a chaperone domain into the prolyl isomerase domain of human FKBP12.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 21510665
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: 22 Apr 2015 08:16
Last Modified: 11 Jun 2015 07:37
URI: https://eref.uni-bayreuth.de/id/eprint/10551