Abstract
Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In eukaryotes, the formation and rearrangement of most intra- and intermolecular disulfide bonds in the endoplasmic reticulum (ER) are mediated by protein disulfide isomerases (PDIs), which consist of multiple thioredoxin-like domains. These domains assist correct folding of proteins, as well as effectively prevent the aggregation of misfolded ones. Protein misfolding often leads to the formation of pathological protein aggregations that cause many diseases. On the other hand, glutenin aggregation and subsequent crosslinking are required for the formation of a rheologically dominating gluten network. Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly. This review systematically illustrated the process of human protein disulfide isomerase (hPDI) mediated disulfide bond formation and complemented this with the current mechanism of wheat protein disulfide isomerase (wPDI) catalyzed formation of gluten networks.
Highlights
The earliest concept of “protein folding” was raised by Christian B
John Ellis proposed a new notion of protein folding: the folding and assembly of a certain polypeptide chain to form the correct oligomeric structure is ensured by proteins that act as molecular chaperones [2]
We reviewed the mechanism of human protein disulfide isomerase catalyzed oxidative protein folding and the mechanism of wheat protein disulfide isomerase (wPDI)-catalyzed glutenin macropolymers (GMP) formation, for a timely update of protein disulfide isomerases (PDIs) studies
Summary
The earliest concept of “protein folding” was raised by Christian B. Oxidative protein folding is a special protein-folding process accompanied by the formation of disulfide bond(s). It may be the most complicated protein folding scenario, due to the possibility of protein misfolding being increased with increasing cysteine numbers in a protein, where only one disulfide bond pattern is proper for the correct folding [4]. The classic substrate, ribonuclease A, was firstly used to study the oxidative folding catalyzed by enzymes, and since the key catalyst—protein disulfide isomerase (PDI)—. PDI-catalyzed oxidative protein folding is virtually a process in which enzymes interact with substrates and catalyze the formation of native disulfide bonds in the substrate protein. We reviewed the mechanism of human protein disulfide isomerase (hPDI) catalyzed oxidative protein folding and the mechanism of wPDI-catalyzed glutenin macropolymers (GMP) formation, for a timely update of PDI studies
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