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peptidyl-prolyl cis/trans isomerase

Protein Science (1)

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Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)
RALPH GOLBIK, GUNTER FISCHER, ALAN R. FERSHT
Journal:

Protein Science / Volume 8 / Issue 7 / July 1999

Published online by Cambridge University Press:

01 July 1999, pp. 1505-1514

Print publication:

July 1999
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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.