| Type: | Family | Name: | Glutathione degradosome, DUG1 |
| Description: | Glutathione (GSH), the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by the action of gamma-glutamyl transpeptidase. A novel pathway for the degradation of GSH that requires the participation of three previously uncharacterised genes has been identified in Saccharomyces cerevisiae(Baker's yeast). These genes are DUG1 (YFR044c), DUG2 (YBR281c, ), and DUG3 (YNL191w), which contains a glutamine amidotransferase type 2 domain, , and is defective in utilization of glutathione. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolysed by the DUG1 protein (a metallopeptidase), the presence of an unusual peptide bond, such as in GSH, requires the participation of the DUG2, which encodes a protein with a metallopeptidase domain and a large WD40 repeat region and DUG3 gene products as well. The DUG3 gene encodes a protein with a glutamine amidotransferase domain. These three proteins form a GSH degradosomal complex []. This entry represents DUG1, which is a metallopeptidases also known as carnosine dipeptidase II that belong to MEROPS peptidase family M20A (glutamate carboxypeptidase family, clan MH). | Short Name: | GSH_degradosome_DUG1 |
