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

被引：33

作者：

Golbik, R

Fischer, G

Fersht, AR

机构：

[1] Univ Halle Wittenberg, Inst Biochem, Abt Enzymol, D-06120 Halle, Germany

[2] Max Planck Gesell Forderung Wissensch EV, Forsch Stelle Enzymol Prot Faltung, D-06120 Halle, Germany

[3] MRC, Ctr Prot Engn, Cambridge CB2 2QH, England

来源：

PROTEIN SCIENCE | 1999年 / 8卷 / 07期

关键词：

barstar; cyclophilin; enzymology; kinetics; peptidyl-prolyl cis trans isomerase; protein folding; thermodynamics;

D O I：

10.1110/ps.8.7.1505

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 k(cat)/K-M of 254,000 M-1 s(-1). The fast refolding phase is not influenced by the enzyme.

引用

收藏

页码：1505 / 1514

页数：10

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