Family

Type I (cytosolic) L-asparaginase (IPR041725)

Short name: L-asparaginase_I

Overlapping homologous superfamilies

Family relationships

Description

Asparaginases (amidohydrolases, EC:3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This entry represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol [PMID: 889890]. Type I L-asparaginase acts as a dimer [PMID: 15735339]. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase [PMID: 11996000]. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes [PMID: 8898907].

Contributing signatures

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