| Primary Identifier | IPR000246 | Type | Family |
| Short Name | Peptidase_T2 |
| 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 + NH3Glycosylasparaginase 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. |
