Peptidase T2, asparaginase 2 (IPR000246)

Short name: Peptidase_T2

Overlapping homologous superfamilies

Family relationships


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 (EC: are threonine peptidases. Also in this family is L-asparaginase (EC:, which catalyses the following reaction: L-asparagine + H2O = L-aspartate + NH3

Glycosylasparaginase catalyses: N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartate cleaving 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 [PMID: 8877373] and plays a major role in the degradation of glycoproteins.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016787 hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.