asparaginase escherichia coli

Asparaginase Escherichia coli is a recombinant enzyme derived from the bacterium *Escherichia coli* that catalyzes the hydrolysis of the amino acid L-asparagine into L-aspartic acid and ammonia[2]. This enzymatic activity depletes circulating levels of asparagine, an amino acid essential for the survival and proliferation of certain leukemic cells—particularly lymphoblasts in acute lymphoblastic leukemia (ALL)—which are unable to synthesize sufficient amounts themselves[2][5]. By depriving these malignant cells of asparagine, the drug induces apoptotic cell death and exerts its antitumor effect[2][5]. Asparaginase from *E. coli* is used primarily in combination chemotherapy regimens for ALL in both pediatric and adult patients; it may also be studied or used off-label for other malignancies[1][6]. The product is available under several trade names including Elspar and can be administered intramuscularly or intravenously[2][3].

Brand names

Elspar

Other names

L-asparaginaseE. coli L-asparaginaseEscherichia coli L-asparagine amidohydrolaseEC 3.5.1.1EC3.5.1.1EC-3.5.1.1