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

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

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1PGS, 1PNF, 1PNG, 1X3W, 1X3Z, 2D5U, 2F4M, 2F4O, 2G9F, 2G9G, 2HPJ, 2HPL, and 2I74.

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.^[2]

References

Further reading