巴氏杆菌C40A/C82A/P27A的折叠以及人胞质亲环蛋白（Cyp18）对肽基脯氨酰顺反异构化的催化作用。
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).
作者信息
Golbik R, Fischer G, Fersht A R
机构信息
Martin-Luther-Universität Halle-Wittenberg, Institut für Biochemie, Abteilung Enzymologie, Halle/Saale, Germany.
出版信息
Protein Sci. 1999 Jul;8(7):1505-14. doi: 10.1110/ps.8.7.1505.
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/K(M) of 254,000 M(-1) s(-1). The fast refolding phase is not influenced by the enzyme.
摘要
b*C40A/C82A/P27A的重折叠由几个动力学上可检测到的折叠阶段组成。重折叠过程中最慢的阶段源于天然状态下处于顺式构象的Tyr47-Pro48肽键的反式→顺式异构化。肽基脯氨酰顺反异构酶人胞质亲环蛋白（Cyp18）可加速这个重折叠阶段，其催化常数与米氏常数的比值（kcat/K(M)）为254,000 M⁻¹ s⁻¹。快速重折叠阶段不受该酶影响。
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