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MDPI, International Journal of Molecular Sciences, 1(16), p. 1791-1805, 2015

DOI: 10.3390/ijms16011791

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Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins

Journal article published in 2015 by Nitin A. Patil ORCID, Julien Tailhades, Richard Anthony Hughes, Frances Separovic ORCID, John D. Wade, Mohammed Akhter Hossain
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of enzymes—a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor—that function inside the cell dictates the formation and maintenance of disulfide bonds. The main pathways that catalyze disulfide bond formation in peptides and proteins in prokaryotes and eukaryotes are remarkably similar and share several mechanistic features. This review summarizes the formation of disulfide bonds in peptides and proteins by cellular and recombinant machinery.