title: Prolyl isomerases show low sequence specificity toward the residue following the proline.
abstract: 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.
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, Bayreuth, Germany.
authors.forename: Philipp A M
authors.initials: PA
authors.lastname: Schmidpeter
authors.forename: Günther
authors.initials: G
authors.lastname: Jahreis
authors.forename: Anne-Juliane
authors.initials: AJ
authors.lastname: Geitner
authors.forename: Franz X
authors.initials: FX
authors.lastname: Schmid
mesh_terms: D006801:Humans; D008958:Models, Molecular; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D011392:Proline / Q000378:metabolism*
chemical_list: D011392:Proline; D019696:Peptidylprolyl Isomerase