2005•Progress in biotechnologyRequires access

Protein Disulfide Isomerase

Zhimin Liu

Abstract

The formation of native disulfide bond is critical for the proper folding of many proteins. It maintains the integrity of protein structure and activity. This review focuses on one of important protein folding assistants- protein disulfide isomerase in endoplasmic reticulum. PDI, an enzyme that catalyzes disulfide formation and rearrangement of incorrect disulfide, behaves as a chaperone inhabiting the aggregation of misfolded proteins. It has a wide application in the expression of heterlogous proteins in eukaryotic hosts.

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Available abstract

Key concepts: Protein disulfide-isomerase, Endoplasmic reticulum, Disulfide bond, Protein folding, Chaperone (clinical), Chemistry, Foldase, Folding (DSP implementation)