Member database | PANTHER |
PANTHER type | family |
Description Imported from IPR000246
Glycosylasparaginases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. They catalyse:
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartate
It cleaves the GlcNAc-Asn bond that links oligosaccharides to asparagine in N-linked glycoproteins. The enzyme is composed of two non-identical alpha/beta subunits joined by strong non-covalent forces, has one glycosylation site located in the alpha subunit
[1] and plays a major role in the degradation of glycoproteins.
L-asparaginases catalyse the following reaction:
L-asparagine + H2O = L-aspartate + NH3
References Imported from IPR000246
1.Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda. Liu Y, Dunn GS, Aronson NN Jr. Glycobiology 6, 527-36, (1996). View articlePMID: 8877373