Protein Domain : Peptidase T2, asparaginase 2 IPR000246

Type	Family
Description	Threonine peptidases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. The threonine peptidases belong to clan PB or are unassigned, clan T-. The type example for this clan is the archaean proteasome beta component of Thermoplasma acidophilum.This group of sequences have a signature that places them in MEROPS peptidase family T2 (clan PB(T)). The glycosylasparaginases ( ) are threonine peptidases. Also in this family is L-asparaginase ( ), which catalyses the following reaction: L-asparagine + H2O = L-aspartate + NH 3Glycosylasparaginase catalyses: N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartatecleaving 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 and has one glycosylation site located in the alpha subunit [] and plays a major role in the degradation of glycoproteins.
Short Name	Peptidase_T2