Endoglycosidases acting on carbohydrate moieties of glycoproteins: Demonstration in mammalian tissue

Nishigaki, Masanori; Muramatsu, Takashi; Kobata, Akira

doi:10.1016/s0006-291x(74)80027-6

Cited by 86 publications

(22 citation statements)

References 12 publications

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“…Expressing the protein in mammalian cells and detection of the activity in the extract confirmed that the human candidate protein is indeed an ENGase. Although the cytosolic ENGase had previously been detected and biochemically characterized (20)(21)(22)(23)(24), the gene encoding this cytosolic enzyme has not been reported. There are two types of cytosolic deglycosylating enzymes that can generate free OSs from glycoproteins (7,8).…”

Section: Discussionmentioning

confidence: 99%

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Endo-β- N -acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol

Suzuki

Yano

Sugimoto

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

126

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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-␤-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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Section: Discussionmentioning

confidence: 99%

“…This cytosolic enzyme activity has been described in a wide variety of animal cells (20)(21)(22)(23)(24). The combined actions of ENGase and a cytosolic ␣-mannosidase (18,19) were found to be essential for free OSs to be transferred into lysosome, where they are further degraded (25).…”

mentioning

confidence: 99%

Endo-β- N -acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol

Suzuki

Yano

Sugimoto

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

126

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“…The first evidence of the occurrence of an N-glycan-ENGase activity in a mammalian tissue was reported in 1974 [99] but the enzyme was not simultaneously purified. A similar enzyme was partially purified from hen oviduct [100] and later purified to homogeneity and further characterised [101].…”

Section: Animal N-glycan-engasesmentioning

confidence: 99%

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

Karamanos¹

2013

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Abstract:Since the discovery of endo-N-acetyl-β-D-glucosaminidases (ENGase) and peptide-N4-(N-acetyl-β-D-glucosaminyl) asparagine amidases (PNGase) most of the published work described their use for structural studies. Less attention was given to the potential roles of those enzymes in the physiology of the cells/organisms they produced them. The scope of this review is firstly to analyse the data on the occurrence and characteristics of murein-, chitin-, and N-glycan-ENGases acting on GlcNAc-containing polymers in three structural families, namely murein, chitin, and N-glycosylproteins, and of PNGases, only acting on N-glycosylproteins, and secondly to discuss the biological roles of the enzymes in the producing cells. The analysis demonstrates the remarkable diversity of the enzymes, and simultaneously the interest of studying their substrate specificity and their structural features. Many examples illustrate the importance of the structure/function relationships studies. Diverse biological roles were anticipated, e.g. they are useful for feeding purposes, are implicated in pathogenesis processes, modulate the activity of macromolecules, and help in the destruction of misfolded proteins. Their effect can be direct or indirect, through the reaction products. Current knowledge only partially explains the biological roles of ENGases and PNGases, thus further studies are expected for determining novel possibilities and elucidating other cell pathways.

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“…Such enzymatic activities (ENGase or chitobiase) have been previously described in various animal cell extracts. ENGase activity wasˆrst identiˆed in 1974 in mammalian cells from rats and pigs by Kobata's group (38). Since then, several research groups have demonstrated that the activity is localized in the cytosol and is involved in the catabolism of glycoproteins (39,41).…”

Section: Endo-b-n-acetylglucosaminidase Processes Foss In the Cytosolmentioning

confidence: 99%

Generation and Metabolism of Cytosolic Free Oligosaccharides in Caenorhabditis elegans

Katoh

Ashida

Yamamoto

2009

TIGG

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Free oligosaccharides (FOSs) found in the cytosol of eukaryotic cells are produced by the enzymatic degradation of dolichol-linked intermediates of N-linked glycosylation and/or by the action of cytosolic peptide:Nglycanases that are involved in the process of endoplasmic reticulum-associated degradation (ERAD) of glycoproteins. FOSs are subsequently trimmed by cytosolic endo-b-N-acetylglucosaminidase and a-mannosidase and then ultimately transferred to the lysosome for degradation into monosaccharides. In this minireview, we describe the formation, catabolism, and possible physiological roles of FOSs and present the results of our study on the structure and function of enzymes associated with the generation of FOSs in the nematode Caenorhabditis elegans.

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Endoglycosidases acting on carbohydrate moieties of glycoproteins: Demonstration in mammalian tissue

Cited by 86 publications

References 12 publications

Endo-β- N -acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol

Endo-β- N -acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol

Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

Generation and Metabolism of Cytosolic Free Oligosaccharides in Caenorhabditis elegans

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