Both the Isomerase and Chaperone Activities are Required for Protein Disulfide Isomerase as a Foldase

机译：蛋白质二硫键异构酶作为折叠酶需要异构酶和伴侣活性

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Protein disulfide isomerase(PDI) is one of the two foldases so far characterized. It is a multifunctional protein in the endoplasmic reticulum at high concentration and is capable of peptide binding with low specificity. It has been suggested to be both an isomerase and a molecular chaperone. PDI at stoichiometric amount increases reactivation and decreases aggregation during refolding of denatured proteins containing no disulfide bond, such as D-glyceraldehyde-3-phosphate dehydrogenase and rhodanese, upon dilution, indicating chaperone activity independent of its isomerase activity. The CGHC-active sites are essential for the isomerase activity but not required for its chaperone activity. The c domain containing the peptide binding site is essential for the chaperone activity.

机译：蛋白质二硫键异构酶（PDI）是迄今为止表征的两种折叠酶之一。它是高浓度内质网中的多功能蛋白，能够以低特异性结合肽。已经有人提出它既是异构酶又是分子伴侣。稀释后，化学计量比的PDI可以增加再活化并减少不含二硫键的变性蛋白质（例如D-甘油醛-3-磷酸脱氢酶和罗丹明）的折叠过程中的聚集，表明分子伴侣活性独立于其异构酶活性。 CGHC活性位点对于异构酶活性是必不可少的，但对于其伴侣蛋白活性却不是必需的。包含肽结合位点的c结构域对于分子伴侣活性是必不可少的。

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《International symposium on mechanisms of enzymatic catalysis》|1998年|28-29|共2页
会议地点 Guilin(CN)
作者
Chih-chen Wang;
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作者单位

National Laboratoiy of Biomacromolecules, Institute of Biophysics,Academia Sinica, Beijing 100101, China;

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原文格式 PDF
正文语种 eng
中图分类 Q-55;
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1. Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor. [J] . Pandhare J, Deshpande V Protein Science: A Publication of the Protein Society . 2004,第9期

机译：蛋白质二硫键异构酶的伴侣和异构酶功能对于加速二聚碱性蛋白酶抑制剂的氧化重折叠和再活化都是必不可少的。
2. Characterization of a Foldase, Protein Disulfide Isomerase A, in the Protein Secretory Pathway ofAspergillus niger [J] . Celina Ngiam, David J. Jeenes, Peter J. Punt, Applied and Environmental Microbiology . 2000,第2期

机译：黑曲霉的蛋白质分泌途径中的折叠酶，蛋白质二硫键异构酶A的表征。
3. Human pancreas-specific protein disulfide-isomerase (PDIp) can function as a chaperone independently of its enzymatic activity by forming stable complexes with denatured substrate proteins. [J] . Fu XM, Zhu BT The Biochemical Journal . 2010,第1期

机译：人胰腺特异性蛋白二硫键异构酶（PDIp）可以通过与变性的底物蛋白形成稳定的复合物而独立于其酶促活性而起分子伴侣的作用。
4. Both the Isomerase and Chaperone Activities are Required for Protein Disulfide Isomerase as a Foldase [C] . International symposium mechanisms of enzymatic catalysis . 1998

机译：蛋白二硫化物异构酶作为重组所需的异构酶和伴侣活性。
5. The Roles of Protein Disulfide-Isomerase Associated 6 and Alpha-B Crystallin in Chaperone-Mediated Cardioprotection. [D] . Vekich, John Alan. 2013

机译：蛋白质相关的二硫键异构酶和α-B晶状体蛋白在伴侣介导的心脏保护中的作用。
6. Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. [O] . Y Yao, Y Zhou, C Wang 1997

机译：蛋白质二硫键异构酶的异构酶和分子伴侣活性对于还原和变性的酸性磷脂酶A2的重新活化都是必需的。
7. Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity [O] . Horibe Tomohisa, Iguchi Daisuke, Masuoka Toshio, 2004

机译：用人类蛋白二硫键异构酶相关结构域b'替换人类蛋白二硫键异构酶相关蛋白的结构域b大大提高了其伴侣蛋白活性

Both the Isomerase and Chaperone Activities are Required for Protein Disulfide Isomerase as a Foldase

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