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Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)

Published online by Cambridge University Press:  01 July 1999

RALPH GOLBIK ,
GUNTER FISCHER  and
ALAN R. FERSHT
RALPH GOLBIK
Affiliation:
Martin-Luther-Universität Halle-Wittenberg, Institut für Biochemie, Abteilung Enzymologie, Kurt-Mothes-Straße 3, Halle/Saale 06120, Germany
GUNTER FISCHER
Affiliation:
Forschungsstelle “Enzymologie der Proteinfaltung,” Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V., Kurt-Mothes-Straße 3, Halle/Saale 06120, Germany
ALAN R. FERSHT
Affiliation:
MRC, Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, United Kingdom
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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/KM of 254,000 M−1 s−1. The fast refolding phase is not influenced by the enzyme.

Keywords

barstarcyclophilinenzymologykineticspeptidyl-prolyl cis/trans isomeraseprotein foldingthermodynamics
Type
Research Article
Information
Protein Science , Volume 8 , Issue 7 , July 1999 , pp. 1505 - 1514
Copyright
© 1999 The Protein Society

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