ArticleProceedings of the National Academy of Sciences of the United States of America2002
Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 147 citations in OpenAlex.
- Deglycosylation at War: Host N-Glycoprotein Remodeling in Infection and Immunity.Infection and drug resistance · 2026Review
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Deciphering the molecular basis of skin color variation through transcriptomics and machine learning.Scientific reports · 2025Article
- Glycosylation in cancer: mechanisms, diagnostic markers, and therapeutic applications.Molecular and cellular biochemistry · 2025Review
- Free oligosaccharides in serum.BBA advances · 2025Article
- Development of new NGLY1 assay systems - toward developing an early screening method for NGLY1 deficiency.Glycobiology · 2024Review
- Genomic diversity and ecological distribution of marineMarine life science & technology · 2023Article
- Biodegradation of Punicalagin into Ellagic Acid by Selected Probiotic Bacteria: A Study of the Underlying Mechanisms by MS-Based Proteomics.Journal of agricultural and food chemistry · 2022Article
- Comparative proteomics reveals elevated CCN2 in NGLY1-deficient cells.Biochemical and biophysical research communications · 2022Article
- Age-Dependent Variations in Functional Quality and Proteomic Characteristics of Canine (International journal of molecular sciences · 2022Article
- A method for assaying peptide: N-glycanase/N-glycanase 1 activities in crude extracts using an N-glycosylated cyclopeptide.Glycobiology · 2022Article
- Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder.American journal of human genetics · 2022Article
- Transcriptome-wide association study reveals two genes that influence mismatch negativity.Cell reports · 2021Article
- N-Glycosylation.Advances in experimental medicine and biology · 2021Article
- Purification, Characterization, and Gene Expression of Rice Endo-β-Frontiers in plant science · 2021Article
- Innovative Preparation of Biopharmaceuticals Using Transglycosylation Activity of Microbial Endoglycosidases.Journal of applied glycoscience · 2021Article
- Cytosolic N-GlcNAc proteins are formed by the action of endo-β-N-acetylglucosaminidase.Biochemical and biophysical research communications · 2020Article
- Loss of N-Glycanase 1 Alters Transcriptional and Translational Regulation in K562 Cell Lines.G3 (Bethesda, Md.) · 2020Article
- Blind killing of both male and female Drosophila embryos by a natural variant of the endosymbiotic bacterium Spiroplasma poulsonii.Cellular microbiology · 2020Article
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8 authors at 1 institution in 1 country.
Funding
Abstract
Formation of oligosaccharides occurs both in the cytosol and in the lumen of the endoplasmic reticulum (ER). Luminal oligosaccharides are transported into the cytosol to ensure that they do not interfere with proper functioning of the glycan-dependent quality control machinery in the lumen of the ER for newly synthesized glycoproteins. Once in the cytosol, free oligosaccharides are catabolized, possibly to maximize the reutilization of the component sugars. An endo-beta-N-acetylglucosaminidase (ENGase) is a key enzyme involved in the processing of free oligosaccharides in the cytosol. This enzyme activity has been widely described in animal cells, but the gene encoding this enzyme activity has not been reported. Here, we report the identification of the gene encoding human cytosolic ENGase. After 11 steps, the enzyme was purified 150,000-fold to homogeneity from hen oviduct, and several internal amino acid sequences were analyzed. Based on the internal sequence and examination of expressed sequence tag (EST) databases, we identified the human orthologue of the purified protein. The human protein consists of 743 aa and has no apparent signal sequence, supporting the idea that this enzyme is localized in the cytosol. By expressing the cDNA of the putative human ENGase in COS-7 cells, the enzyme activity in the soluble fraction was enhanced 100-fold over the basal level, confirming that the human gene identified indeed encodes for ENGase. Careful gene database surveys revealed the occurrence of ENGase homologues in Drosophila melanogaster, Caenorhabditis elegans, and Arabidopsis thaliana, indicating the broad occurrence of ENGase in higher eukaryotes. This gene was expressed in a variety of human tissues, suggesting that this enzyme is involved in basic biological processes in eukaryotic cells.
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