Formation and transfer of disulphide bonds in living cells.
Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of protein disulphide bonds in prokaryotes and eukaryotes are remarkably similar, and they share several mechanistic features. The recent identification of new redox-active proteins in humans and yeast that mechanistically parallel the more established redox-active enzymes indicates that there might be further uncharacterized redox pathways throughout the cell.
Sevier
Carolyn S
CS
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Kaiser
Chris A
CA
D001419:Bacteria / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism; D005415:Flavins / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D011387:Prokaryotic Cells / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D011809:Quinones / Q000378:metabolism
D004220:Disulfides; D005415:Flavins; D011506:Proteins; D011809:Quinones; D005978:Glutathione