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This novel human-like asparaginase is an engineered mammalian enzyme designed to deplete systemic L-asparagine while minimizing the immunogenicity and off-target glutaminase activity associated with traditional bacterial-derived asparaginases (e.g., from *E. coli* or *Erwinia*). Developed by researchers at the University of Illinois Chicago and Ghent University, the enzyme specifically targets asparagine synthetase (ASNS)-deficient cancer cells, which rely on extracellular asparagine for survival. Preclinical studies presented at AACR 2025 demonstrate that this humanized variant achieves durable tumor suppression in models of acute lymphoblastic leukemia (ALL), acute myeloid leukemia (AML), melanoma, and hepatocellular carcinoma. By eliminating glutaminase-driven toxicity, this therapeutic candidate aims to expand the clinical utility of metabolic starvation to a broader range of malignancies beyond pediatric ALL.
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