The Enzyme Database

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Accepted name: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Reaction: Endohydrolysis of the N,N′-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
Other name(s): N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1→4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H
Systematic name: glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
Comments: A group of related enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-88-9
1.  Chien, S., Weinburg, R., Li, S. and Li, Y. Endo-β-N-acetylglucosaminidase from fig latex. Biochem. Biophys. Res. Commun. 76 (1977) 317–323. [DOI] [PMID: 1027432]
2.  Koide, N. and Muramatsu, T. Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. Biol. Chem. 249 (1974) 4897–4904. [PMID: 4152561]
3.  Pierce, R.J., Spik, G. and Montreuil, J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180 (1979) 673. [PMID: 486141]
4.  Pierce, R.J., Spik, G. and Montreuil, J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185 (1980) 261–264. [PMID: 7378051]
5.  Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem. 250 (1975) 8569–8575. [PMID: 389]
6.  Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249 (1974) 818–824. [PMID: 4204553]
[EC created 1978]

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