The Enzyme Database

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EC 3.5.1.52     
Accepted name: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
Reaction: Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue
Other name(s): glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F
Systematic name: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase
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: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 83534-39-8
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 (1981) 10243–10246. [PMID: 7287707]
2.  Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194–1201. [DOI] [PMID: 901470]
3.  Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467–1473. [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 (1985) 4665–4671. [PMID: 4063349]
[EC 3.5.1.52 created 1984, modified 1989 (EC 3.2.2.18 created 1984, incorporated 1989)]
 
 


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