Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2015 Jan 17

PMID 25594871

Citations 19

Authors

Nitin A Patil

Julien Tailhades

Richard Anthony Hughes

Frances Separovic

John D Wade

Mohammed Akhter Hossain

Affiliations

Soon will be listed here.

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.

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