Hostname: page-component-cd9895bd7-jn8rn Total loading time: 0 Render date: 2024-12-28T01:48:11.672Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)