Active Site

Asparaginase/glutaminase, active site 1 (IPR020827)

Short name: Asparaginase/glutaminase_AS1


Asparaginase, which 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]. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma [PMID: 2407723, PMID: 3379033] - if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die. Glutaminase, a similar enzyme, catalyses the deaminination of glutamine to glutamic acid and an ammonium ion [PMID: 2407723]. Both enzymes are homotetramers [PMID: 3026924]: two threonine residues in the N-terminal half of the proteins are involved in the catalytic activity.

Two conserved threonine residues 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 is located at the end of the first third of the sequence. This entry represents the first conserved site.

GO terms

Biological Process

GO:0006520 cellular amino acid metabolic process

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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