| Type: | Active_site | Name: | Asparaginase/glutaminase, active site 1 |
| Description: | 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 []. 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 [, ] - 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 []. Both enzymes are homotetramers []: 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 [, ]. 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. | Short Name: | Asparaginase/glutaminase_AS1 |
