EC 3.5.1.52 - Peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase

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IntEnz Enzyme Nomenclature
EC 3.5.1.52

Names

Accepted name:
peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
Other names:
N-glycanase
N-oligosaccharide glycopeptidase
Jack-bean glycopeptidase
PNGase A
PNGase F
glycopeptidase
glycopeptide N-glycosidase
Systematic name:
N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase

Reaction

Comments:

Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0000224
CAS Registry Number: 83534-39-8
UniProtKB/Swiss-Prot: (22) [show] [UniProt]

References

  1. Plummer, T.H., Jr. and Tarentino, A.L.
    Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase.
    J. Biol. Chem. 256: 10243-10246 (1981). [PMID: 7287707]
  2. Takahashi, N.
    Demonstration of a new amidase acting on glycopeptides.
    Biochem. Biophys. Res. Commun. 76: 1194-1201 (1977). [PMID: 901470]
  3. Takahashi, N. and Nishibe, H.
    Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages.
    J. Biochem. (Tokyo) 84: 1467-1473 (1978). [PMID: 738997]
  4. Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr.
    Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F.
    Biochemistry 24: 4665-4671 (1985). [PMID: 4063349]

[EC 3.5.1.52 created 1984, modified 1989 (EC 3.2.2.18 created 1984, incorporated 1989)]