title: Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).
abstract: Refolding of b*C40A/C82A/P27A is comprised of several kinetically detectable folding phases. The slowest phase in refolding originates from trans-->cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state. This refolding phase can be accelerated by the peptidyl-prolyl cis/trans isomerase human cytosolic cyclophilin (Cyp18) with a kcat/K(M) of 254,000 M(-1) s(-1). The fast refolding phase is not influenced by the enzyme.
authors.affiliation: Martin-Luther-Universität Halle-Wittenberg, Institut für Biochemie, Abteilung Enzymologie, Halle/Saale, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Golbik
authors.forename: G
authors.initials: G
authors.lastname: Fischer
authors.forename: A R
authors.initials: AR
authors.lastname: Fersht
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D002384:Catalysis; D003600:Cytosol / Q000737:chemistry*; D006801:Humans; D007536:Isomerism; D007700:Kinetics; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D019696:Peptidylprolyl Isomerase