Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).
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.
Golbik
R
R
Martin-Luther-Universität Halle-Wittenberg, Institut für Biochemie, Abteilung Enzymologie, Halle/Saale, Germany.
Fischer
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G
Fersht
A R
AR
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
D001426:Bacterial Proteins; D011994:Recombinant Proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D019696:Peptidylprolyl Isomerase