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Cellular disulfide bond formation in bioactive peptides and proteins.

Patil NA, Tailhades J, Hughes RA, Separovic F, Wade JD, Hossain MA - Int J Mol Sci (2015)

Bottom Line: Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics.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.

View Article: PubMed Central - PubMed

Affiliation: Florey Institute of Neuroscience and Mental Health, the University of Melbourne, Victoria 3010, Australia. fs@unimelb.edu.au.

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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Cellular representation of enzyme systems and respective organelles.
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ijms-16-01791-f002: Cellular representation of enzyme systems and respective organelles.

Mentions: The formation of disulfide bonds in bacterial (prokaryotic) cells is well characterized [14,15]. Generally, bacterial proteins are synthesized by ribosomal mRNA translation and disulfide bonds are subsequently formed as posttranslational modifications catalyzed by various enzymes located in the periplasm [16] or cytoplasm [17,18]. In higher animals the same process is performed in specific cell organelles, such as mitochondria, the endoplasmic reticulum (ER) and chloroplasts (Figure 2, Table 1).


Cellular disulfide bond formation in bioactive peptides and proteins.

Patil NA, Tailhades J, Hughes RA, Separovic F, Wade JD, Hossain MA - Int J Mol Sci (2015)

Cellular representation of enzyme systems and respective organelles.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4307334&req=5

ijms-16-01791-f002: Cellular representation of enzyme systems and respective organelles.
Mentions: The formation of disulfide bonds in bacterial (prokaryotic) cells is well characterized [14,15]. Generally, bacterial proteins are synthesized by ribosomal mRNA translation and disulfide bonds are subsequently formed as posttranslational modifications catalyzed by various enzymes located in the periplasm [16] or cytoplasm [17,18]. In higher animals the same process is performed in specific cell organelles, such as mitochondria, the endoplasmic reticulum (ER) and chloroplasts (Figure 2, Table 1).

Bottom Line: Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics.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.

View Article: PubMed Central - PubMed

Affiliation: Florey Institute of Neuroscience and Mental Health, the University of Melbourne, Victoria 3010, Australia. fs@unimelb.edu.au.

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.

Show MeSH
Related in: MedlinePlus