L-asparaginase, N-terminal (IPR027474)

Short name: L-asparaginase_N

Overlapping homologous superfamilies

Domain relationships



This entry represents the N-terminal domain of the L-asparaginase. Each monomer of L-asparaginase is arranged into two easily identifiable domains, the larger N-terminal domain and the smaller C-terminal domain, connected by a linker consisting of approximately 20 residues [PMID: 12499544]. The N-terminal domain covers two conserved threonine residues, which have been shown to play a catalytic role [PMID: 1906013, PMID: 8348975]. One of them is located in the N-terminal extremity while the second one is located at the end of the first third of the sequence.

Asparaginase is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma [PMID: 3026924]. Glutaminase, a similar enzyme, catalyses the deaminination of glutamine to glutamic acid and an ammonium ion [PMID: 2407723]. Both asparaginase and glutaminase contain the domain represented in this entry.

Contributing signatures

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