期刊
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
卷 18, 期 6, 页码 762-769出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2007.09.010
关键词
peptide : N-glycanase; ER-associated degradation; free oligosaccharide; PUB domain
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. (C) 2007 Elsevier Ltd. All rights reserved.
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