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

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peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
Protein NGLY1 PDB 2ccq.png
Rendering based on PDB: 2ccq
Identifiers
EC number 3.5.1.52
CAS number 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

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]

  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 / FEBS. 252 (1): 118–23. PMID 9523720. doi:10.1046/j.1432-1327.1998.2520118.x. 
  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. PMID 16807242. doi:10.1074/jbc.M601173200. 
  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. PMC 4367255Freely accessible. PMID 25614628. doi:10.1074/jbc.M114.605493. 

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. PMID 7287707. 
  • Takahashi N (Jun 1977). "Demonstration of a new amidase acting on glycopeptides". Biochemical and Biophysical Research Communications. 76 (4): 1194–201. PMID 901470. doi:10.1016/0006-291X(77)90982-2. 
  • Takahashi N, Nishibe H (Dec 1978). "Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages". Journal of Biochemistry. 84 (6): 1467–73. PMID 738997. doi:10.1093/oxfordjournals.jbchem.a132270. 
  • Tarentino AL, Gómez CM, Plummer TH (Aug 1985). "Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F". Biochemistry. 24 (17): 4665–71. PMID 4063349. doi:10.1021/bi00338a028.