Article
Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment.
International journal of biological macromolecules - 1 Dec 2018
Aghaeepoor Mojtaba, Akbarzadeh Ali, Mirzaie Sako, Hadian Asieh, Jamshidi Aval Sanaz, Dehnavi Ehsan
Abstract excerpt
Type II l‑asparaginase (l‑ASNase) is an FDA approved enzyme drug with extensive applications for treatment of certain blood cancers. However, the therapeutic efficiency of this enzyme is hampered by its undesirable glutaminase activity. Given the pivotal role of this enzyme against cancer, designing engineered mutants with diminished glutaminase activity would be of great therapeutic interest. To this end, N248S...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Asparaginase
- Catalytic Domain
- Enzyme Stability
- Glutaminase
- Kinetics
- Molecular Docking Simulation
- Molecular Dynamics Simulation
- Mutagenesis, Site-Directed
- Mutation
- Precursor Cell Lymphoblastic Leukemia-Lymphoma