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Extracellular L-asparagine is a naturally occurring amino acid found in plasma and other body fluids. In normal physiology, it is used for protein synthesis and is taken up by cells via amino acid transporters. Certain malignancies, notably acute lymphoblastic leukemia, are unable to synthesize sufficient intracellular asparagine and depend on extracellular supplies. Drugs such as L-asparaginase exploit this vulnerability by enzymatically depleting the extracellular pool of L-asparagine, thereby starving leukemic cells and inducing apoptosis[3][4][5][6]. While extracellular L-asparagine itself is not a molecular drug target, its concentration serves as a functional biomarker and therapeutic substrate.\n\nExtracellular L-asparagine should not be listed as a canonical drug target; instead, the relevant protein target is "L-asparaginase," the enzyme used therapeutically to hydrolyze extracellular L-asparagine in certain diseases, most notably ALL[4][5][6].
Enzymatic hydrolysis: L-asparaginase catalyzes conversion of extracellular L-asparagine to aspartic acid and ammonia, depriving cells (notably leukemic lymphoblasts) of asparagine necessary for protein synthesis
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