Beta-aspartyl-N-acetylglucosaminidase
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| beta-aspartyl-N-acetylglucosaminidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.2.11 | ||||||||
| CAS no. | 9027-31-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction
- 1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O L-asparagine + N-acetyl-D-glucosamine
Thus, the two substrates of this enzyme are 1-beta-aspartyl-N-acetyl-D-glucosaminylamine and H2O, whereas its two products are L-asparagine and N-acetyl-D-glucosamine. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is 1-beta-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase. This enzyme is also called beta-aspartylacetylglucosaminidase.
References
- Eylar EH, Murakami M (1966). "β-Aspartyl-N-acetylglucosaminadase from epididymis". Complex Carbohydrates. Methods in Enzymology. Vol. 8. pp. 597–600. doi:10.1016/0076-6879(66)08107-2. ISBN 978-0-12-181808-1.
