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Background: Cancer is one of the leading causes of death in children and adolescents, with a significant concentration in low and middle-income countries. Previous research has identified disparities in cancer incidence and mortality based on a country's level of development. The Middle East and North Africa (MENA) region comprises of countries with heterogeneous income and development levels.

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A human-like glutaminase-free asparaginase is highly efficacious in ASNS leukemia and solid cancer mouse xenograft models.

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Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, USA; Enzyme By Design Inc., Chicago, USA; Research Biologist, Biological Science Research and Development, Department of Veterans Affairs Medical Center, Chicago, IL, USA. Electronic address:

L-asparaginase (L-ASNase) is crucial in treating pediatric acute lymphoblastic leukemia (ALL), but its use is hampered by side effects from the immunogenicity and L-glutaminase (L-GLNase) co-activity of FDA-approved bacterial L-ASNases, often leading to treatment discontinuation and poor outcomes. The toxicity of these L-ASNases makes them especially challenging to use in adult cancer patients. To overcome these issues, we developed EBD-200, a humanized guinea pig L-ASNase with low Km and no L-GLNase activity, eliminating glutamine-related toxicity.

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