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The role of Glu73 of barnase in catalysis and the binding of barstar.核糖核酸酶 barnase 的 Glu73 在催化作用及与核糖核酸酶抑制蛋白 barstar 结合中的作用。
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The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin.钙调节激素降钙素的顺式/反式相互转化由亲环蛋白催化。
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Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation.工程化二硫键作为核糖核酸酶Barnase折叠途径的探针:提高蛋白质对变性速率的稳定性。
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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.

DOI:10.1110/ps.8.7.1505
PMID:10422840
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2144385/
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。