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Yeast N-glycanase distinguishes between native and non-native glycoproteins.
- Source :
-
EMBO reports [EMBO Rep] 2004 Feb; Vol. 5 (2), pp. 201-6. Date of Electronic Publication: 2004 Jan 09. - Publication Year :
- 2004
-
Abstract
- N-glycanase from Saccharomyces cerevisiae (Png1) preferentially removes N-glycans from misfolded proteins. The ability of Png1 to distinguish between folded and misfolded glycoproteins is reminiscent of substrate recognition by UDP-glucose glycoprotein glucosyl transferase, an enzyme that possesses this trait. The only known in vivo substrates of Png1 are aberrant glycoproteins that originate in the endoplasmic reticulum, and arrive in the cytoplasm for proteasomal degradation. The substrate specificity of Png1 is admirably suited for this task.
- Subjects :
- Cell Line
Glycoproteins chemistry
Glycoside Hydrolases chemistry
Glycoside Hydrolases metabolism
Glycosylation
Humans
Mutation genetics
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase chemistry
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase isolation & purification
Protein Conformation
Protein Folding
Ribonucleases chemistry
Ribonucleases metabolism
Saccharomyces cerevisiae Proteins chemistry
Saccharomyces cerevisiae Proteins isolation & purification
Substrate Specificity
alpha 1-Antitrypsin chemistry
alpha 1-Antitrypsin genetics
alpha 1-Antitrypsin metabolism
Glycoproteins metabolism
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase metabolism
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1469-221X
- Volume :
- 5
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- EMBO reports
- Publication Type :
- Academic Journal
- Accession number :
- 14726951
- Full Text :
- https://doi.org/10.1038/sj.embor.7400066