期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 16, 期 1, 页码 1791-1805出版社
MDPI
DOI: 10.3390/ijms16011791
关键词
bioactive peptides; disulfide bonds; peptide and protein folding; oxidative folding; recombinant technology
资金
- NHMRC (Australia) [1023321]
- ARC [LP120100654]
- Victorian Government's Operational Infrastructure Support Program
- University of Melbourne
- Australian Research Council [LP120100654] Funding Source: Australian Research Council
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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