N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
From Wikipedia the free encyclopedia
| N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.45 | ||||||||
| CAS no. | 75788-84-0 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase (EC 3.1.4.45)[1][2][3] catalyzes the reaction
- glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase. Other names in common use include α-N-acetylglucosaminyl phosphodiesterase, lysosomal α-N-acetylglucosaminidase, phosphodiester glycosidase, α-N-acetyl-D-glucosamine-1-phosphodiester, N-acetylglucosaminidase, 2-acetamido-2-deoxy-α-D-glucose 1-phosphodiester, and acetamidodeoxyglucohydrolase.
References[edit]
- ^ van der Drift C, van Helvoort PE, Vogels GD (1971). "S-ureidoglycolate dehydrogenase: purification and properties". Arch. Biochem. Biophys. 145 (2): 465–9. doi:10.1016/S0003-9861(71)80006-1. PMID 4399430.
- ^ Van der Drift L, Vogels GD, Van der Drift C (1975). "Allantoin racemase: a new enzyme from Pseudomonas species". Biochim. Biophys. Acta. 391 (1): 240–8. doi:10.1016/0005-2744(75)90170-9. PMID 237557.
- ^ Waheed A, Hasilik A, von Figura K (1981). "Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal α-N-acetylglucosaminyl phosphodiesterase". J. Biol. Chem. 256 (11): 5717–21. PMID 6263889.
