EC 3.2.1.96 - Mannosyl-glycoprotein endo-β-N-acetylglucosaminidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.96

Names

Accepted name:
mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Other names:
N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase
di-N-acetylchitobiosyl β-N-acetylglucosaminidase
endo-N-acetyl-β-D-glucosaminidase
endo-N-acetyl-β-glucosaminidase
endo-β-(1→4)-N-acetylglucosaminidase
endo-β-N-acetylglucosaminidase
endo-β-N-acetylglucosaminidase D
endo-β-N-acetylglucosaminidase F
endo-β-N-acetylglucosaminidase H
endo-β-N-acetylglucosaminidase L
endo-β-acetylglucosaminidase
endoglycosidase S
mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase
mannosyl-glycoprotein endo-β-N-acetylglucosamidase
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

Reaction

Comments:

A group of related enzymes.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00839
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033925
CAS Registry Number: 37278-88-9
UniProtKB/Swiss-Prot: (27) [show] [UniProt]

References

  1. Chien, S., Weinburg, R., Li, S. and Li, Y.
    Endo-β-N-acetylglucosaminidase from fig latex.
    Biochem. Biophys. Res. Commun. 76: 317-323 (1977).
  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: 4897-4904 (1974). [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: 673 (1979). [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: 261-264 (1980). [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: 8569-8575 (1975). [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: 818-824 (1974). [PMID: 4204553]

[EC 3.2.1.96 created 1978]