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Peptide N4 (N acetyl beta glucosaminyl)asparagine amidase

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EC number
  
3.5.1.52

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
83534-39-8

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

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.

Contents

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, and
  • PNGase F
  • Structural studies

    The enzyme uses a catalytic triad of cysteine-histidine-aspartate in its active site for hydrolysis by covalent catalysis. 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.

    References

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