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蛋白质二硫键异构酶作为一种异构酶和伴侣蛋白协助蛋白质折叠。

Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone.

作者信息

Wang C C

机构信息

National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.

出版信息

Ann N Y Acad Sci. 1998 Dec 13;864:9-13. doi: 10.1111/j.1749-6632.1998.tb10283.x.

DOI:10.1111/j.1749-6632.1998.tb10283.x
PMID:9928079
Abstract

Protein disulfide isomerase (PDI) is the physiological catalyst of native disulfide bond formation of nascent peptides in the cells. As a foldase, PDI has both isomerase and chaperone activities. The chaperone activity is intrinsic and independent of its isomerase activity. Both chaperone and isomerase activities are required for PDI to assist folding of denatured and reduced disulfide-containing proteins. PDI may have great applications in protein production by bioengineering for its function as a foldase.

摘要

蛋白质二硫键异构酶(PDI)是细胞中新生肽天然二硫键形成的生理催化剂。作为一种折叠酶,PDI具有异构酶和伴侣蛋白活性。伴侣蛋白活性是内在的,且独立于其异构酶活性。PDI协助变性和还原的含二硫键蛋白质折叠需要伴侣蛋白和异构酶活性。由于其作为折叠酶的功能,PDI在生物工程蛋白质生产中可能有很大的应用。

相似文献

1
Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone.蛋白质二硫键异构酶作为一种异构酶和伴侣蛋白协助蛋白质折叠。
Ann N Y Acad Sci. 1998 Dec 13;864:9-13. doi: 10.1111/j.1749-6632.1998.tb10283.x.
2
Isomerase and chaperone activities of protein disulfide isomerase are both required for its function as a foldase.蛋白质二硫键异构酶作为一种折叠酶发挥功能时,其异构酶活性和伴侣活性都是必需的。
Biochemistry (Mosc). 1998 Apr;63(4):407-12.
3
Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor.蛋白质二硫键异构酶的伴侣功能和异构酶功能对于加速二聚体碱性蛋白酶抑制剂的氧化重折叠和再激活都是必不可少的。
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Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.还原变性的酸性磷脂酶A2的再活化需要蛋白质二硫键异构酶的异构酶活性和伴侣活性。
EMBO J. 1997 Feb 3;16(3):651-8. doi: 10.1093/emboj/16.3.651.
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The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.硫醇/二硫键中心和肽结合位点在蛋白质二硫键异构酶的伴侣和抗伴侣活性中的作用。
J Biol Chem. 1994 Jul 22;269(29):19128-35.
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Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.蛋白二硫键异构酶在不依赖其肽结合活性的情况下使人胰岛素原中的非天然二硫键异构化。
Protein Sci. 2011 Mar;20(3):588-96. doi: 10.1002/pro.592.
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Chaperone activity of DsbC.DsbC的伴侣活性。
J Biol Chem. 1999 Jul 9;274(28):19601-5. doi: 10.1074/jbc.274.28.19601.
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Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase.以酸变性绿色荧光蛋白(GFP)作为模型底物来研究蛋白质二硫键异构酶的伴侣活性。
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Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme.在蛋白质二硫键异构酶催化还原变性溶菌酶重折叠过程中BiP的抗伴侣蛋白行为。
J Biol Chem. 1994 Oct 14;269(41):25889-96.
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Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.蛋白质二硫键异构酶在溶菌酶的氧化重折叠过程中表现出伴侣活性和抗伴侣活性。
J Biol Chem. 1994 Mar 11;269(10):7764-71.

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