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

In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase 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 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, and PNGase F.

Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , and.