EC |
3.5.1.26 |
Accepted name: |
N4-(β-N-acetylglucosaminyl)-L-asparaginase |
Reaction: |
N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-β-D-glucosaminylamine + L-aspartate |
Other name(s): |
aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase |
Systematic name: |
N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase |
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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9075-24-5 |
References: |
1. |
Kohno, M. and Yamashina, I. Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney. Biochim. Biophys. Acta 258 (1972) 600–617. [DOI] [PMID: 5010303] |
2. |
Mahadevan, S. and Tappel, A.L. β-Aspartylglucosylamine amido hydrolase of rat liver and kidney. J. Biol. Chem. 242 (1967) 4568–4576. [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 (1969) 295–303. [PMID: 5778645] |
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[EC 3.5.1.26 created 1972 (EC 3.5.1.37 created 1972, incorporated 1976)] |
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