Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)
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DOI：
10.1110/ps.8.7.1505
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发表时间：
1999-07-01
期刊：
影响因子：
8
通讯作者：
Fersht, AR
中科院分区：
文献类型：
--
作者：
Golbik, R;Fischer, G;Fersht, AR
b*C40A/C82A/P27A的再折叠由几个动力学可检测的折叠相组成。重折叠的最慢阶段源于Tyr47-Pro48肽键的反式->顺式异构化，在天然状态下呈顺式构象。肽基脯氨酸顺式/反式异构酶human cytosolic cyclophilin （Cyp18）可以加速这个重折叠阶段，其k(cat)/ k - m为254,000 M-1 s（-1）。快速再折叠阶段不受酶的影响。
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.