Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
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| peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.5.1.52 | ||||||||
| CAS no. | 83534-39-8 | ||||||||
| 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 | ||||||||
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In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides.
The NGLY1 gene encodes the ortholog of this enzyme in humans.
Nomenclature
[edit]The systematic name of this enzyme class is N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase. Other names in common use include:
- glycopeptide N-glycosidase,
- glycopeptidase,
- N-oligosaccharide glycopeptidase,
- N-glycanase,
- Jack-bean glycopeptidase,
- PNGase A,[1] and
- PNGase F
Structural studies
[edit]The enzyme uses a catalytic triad of cysteine-histidine-aspartate in its active site for hydrolysis by covalent catalysis.[2] A peptide with similar functionality was discovered in 2014 by group at Fudan University in Shanghai, China. This peptide also cleaves alpha 1,3 linkages, and has been named PNGase F-II.[3]
References
[edit]- ^ Altmann F, Paschinger K, Dalik T, Vorauer K (Feb 1998). "Characterisation of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A and its N-glycans". European Journal of Biochemistry. 252 (1): 118–23. doi:10.1046/j.1432-1327.1998.2520118.x. PMID 9523720.
- ^ Allen MD, Buchberger A, Bycroft M (Sep 2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". The Journal of Biological Chemistry. 281 (35): 25502–8. doi:10.1074/jbc.M601173200. PMID 16807242.
- ^ Sun G, Yu X, Bao C, Wang L, Li M, Gan J, Qu D, Ma J, Chen L (Mar 2015). "Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningoseptica". The Journal of Biological Chemistry. 290 (12): 7452–62. doi:10.1074/jbc.M114.605493. PMC 4367255. PMID 25614628.
Further reading
[edit]- Plummer TH, Tarentino AL (Oct 1981). "Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase". The Journal of Biological Chemistry. 256 (20): 10243–6. doi:10.1016/S0021-9258(19)68610-2. PMID 7287707.
- Takahashi N (Jun 1977). "Demonstration of a new amidase acting on glycopeptides". Biochemical and Biophysical Research Communications. 76 (4): 1194–201. doi:10.1016/0006-291X(77)90982-2. PMID 901470.
- Takahashi N, Nishibe H (Dec 1978). "Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages". Journal of Biochemistry. 84 (6): 1467–73. doi:10.1093/oxfordjournals.jbchem.a132270. PMID 738997.
- Tarentino AL, Gómez CM, Plummer TH (Aug 1985). "Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F". Biochemistry. 24 (17): 4665–71. doi:10.1021/bi00338a028. PMID 4063349.
