EC 3.5.1.26 - N4-(β-N-acetylglucosaminyl)-L-asparaginase

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IntEnz Enzyme Nomenclature
EC 3.5.1.26

Names

Accepted name:
N4-(β-N-acetylglucosaminyl)-L-asparaginase
Other names:
N-aspartyl-β-glucosaminidase
β-aspartylglucosylamine amidohydrolase
aspartylglucosaminidase
aspartylglucosylaminase
aspartylglucosylamine deaspartylase
aspartylglycosylamine amidohydrolase
glucosylamidase
glycosylasparaginase
aspartylglucosylaminidase
4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Systematic name:
N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase

Reaction

Comments:

Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52 peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003948
CAS Registry Number: 9075-24-5
UniProtKB/Swiss-Prot: (17) [show] [UniProt]

References

  1. Kohno, M. and Yamashina, I.
    Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney.
    Biochim. Biophys. Acta 258: 600-617 (1972). [PMID: 5010303]
  2. Mahadevan, S. and Tappel, A.L.
    β-Aspartylglucosylamine amido hydrolase of rat liver and kidney.
    J. Biol. Chem. 242: 4568-4576 (1967). [PMID: 6061403]
  3. Tarentino, A.L. and Maley, F.
    The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct.
    Arch. Biochem. Biophys. 130: 295-303 (1969). [PMID: 5778645]

[EC 3.5.1.26 created 1972 (EC 3.5.1.34 created 1972, incorporated 1981)]