کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2203344 | 1100438 | 2007 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol](/preview/png/2203344.png)
Peptide:N-glycanase (PNGase) releases N-glycans from glycoproteins/glycopeptides. Cytoplasmic PNGase is widely recognized as a component of machinery for ER-associated degradation (ERAD), i.e. proteasomal degradation of misfolded, newly synthesized (glyco)proteins that have been exported from the ER. The enzyme belongs to the “transglutaminase superfamily” that contains a putative catalytic triad of cysteine, histidine, and aspartic acid. The mammalian orthologues of PNGase contain the N-terminal PUB domain that serves as the protein–protein interaction domain. The C-terminus of PNGase was recently found to be a novel carbohydrate-binding domain. Taken together, these observations indicate that C-terminus of mammalian PNGase is important for recognition of the substrates while N-terminus of this enzyme is involved in assembly of a degradation complex.
Journal: Seminars in Cell & Developmental Biology - Volume 18, Issue 6, December 2007, Pages 762–769