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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.

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。

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