In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC3.5.1.52) 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:
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]
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. PMID901470.
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. PMID738997.
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. PMID4063349.
