Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
Rendering based on PDB: 2ccq ​
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
Search PMC articles PubMed articles NCBI proteins

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

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

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

1. 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.
2. 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.
3. 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

• 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. Bibcode:1977BBRC...76.1194T. 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.