| Description | L-asparaginase catalyses the conversion of L-asparagine to L-aspartate. Two related families of asparaginase (L-asparagine amidohydrolase, ) are designated type I and type II according to the terminology in Escherichia coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This family describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers [ ]. 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 [].Type II L-asparaginases are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects [ ]. Tumour cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells []. | Name | L-asparaginase, type II |
| Short Name | AsnASE_II | Type | Family |
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