ArticlePloS one2016
Purification and Characterization of Glutaminase Free Asparaginase from Enterobacter cloacae: In-Vitro Evaluation of Cytotoxic Potential against Human Myeloid Leukemia HL-60 Cells.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.
- A systematic review of recent trends in research on therapeutically significant L-asparaginase and acute lymphoblastic leukemia.Molecular biology reports · 2022Pooled it
- Novel glutaminase-free l-asparaginase fromRSC advances · 2026Article
- Recombinant L-asparaginase from Stenotrophomonas maltophilia: a promising low-immunogenic anticancer agent.Microbial cell factories · 2025Article
- Characterization and bioactivities of glutaminase-free L-asparaginase from Salinicola acorporae S4-41.Microbial cell factories · 2025Article
- Molecular Mechanisms and Therapeutic Perspectives of Gut Microbiota, Autophagy, and Apoptosis in Cholangiocarcinoma Pathophysiology.International journal of molecular sciences · 2025Review
- Biochemical and biological evaluation of L-glutaminase from Aspergillus tamarii AUMC 10198 via solid-state fermentation.Microbial cell factories · 2025Article
- Tapping the untapped: type II L-asparaginase from marine crustacean-derived Chryseomicrobium amylolyticum as a potential bio better for blood cancer therapy.Scientific reports · 2025Article
- L-asparaginase from the mangrove endophyteToxicology research · 2025Article
- Enhanced production and purification of L-asparaginase from Bacillus paralicheniformis AUMC B-516 with potent cytotoxicity against MCF-7 cell lines.AMB Express · 2025Article
- Cytotoxicity of L-asparaginase from eucaryotic Cladosporium species against breast and colon cancer in vitro.Journal of the Egyptian National Cancer Institute · 2025Article
- Isolation and Characterization of L-Asparaginase-Producing Bacteria from the Arabian-Persian Gulf Region: First Report onMarine drugs · 2025Article
- The human microbiome: redefining cancer pathogenesis and therapy.Cancer cell international · 2025Review
- L-asparaginase from the novel Fusarium falciforme AUMC 16563: extraction, purification, characterization, and cytotoxic effects on PC-3, HePG-2, HCT-116, and MCF-7 cell lines.BMC microbiology · 2025Article
- Nonclinical Evaluation of Single-MutantInternational journal of molecular sciences · 2024Article
- Substrate Affinity Is Not Crucial for Therapeutic L-Asparaginases: Antileukemic Activity of Novel Bacterial Enzymes.Molecules (Basel, Switzerland) · 2024Article
- Production of highly cytotoxic and low immunogenic L-asparaginase from Stenotrophomonas maltophilia EMCC2297.AMB Express · 2024Article
- Enzyme Engineering Strategies for the Bioenhancement of L-Asparaginase Used as a Biopharmaceutical.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- A Novel Formulation of Asparaginase Encapsulated into Virus-like Particles of Brome Mosaic Virus: In Vitro and In Vivo Evidence.Pharmaceutics · 2023Article
- Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics.AMB Express · 2023Article
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Asparaginase is an important antileukemic agent extensively used worldwide but the intrinsic glutaminase activity of this enzymatic drug is responsible for serious life threatening side effects. Hence, glutaminase free asparaginase is much needed for upgradation of therapeutic index of asparaginase therapy. In the present study, glutaminase free asparaginase produced from Enterobacter cloacae was purified to apparent homogeneity. The purified enzyme was found to be homodimer of approximately 106 kDa with monomeric size of approximately 52 kDa and pI 4.5. Purified enzyme showed optimum activity between pH 7-8 and temperature 35-40°C, which is close to the internal environment of human body. Monovalent cations such as Na+ and K+ enhanced asparaginase activity whereas divalent and trivalent cations, Ca2+, Mg2+, Zn2+, Mn2+, and Fe3+ inhibited the enzyme activity. Kinetic parameters Km, Vmax and Kcat of purified enzyme were found to be 1.58×10-3 M, 2.22 IU μg-1 and 5.3 × 104 S-1, respectively. Purified enzyme showed prolonged in vitro serum (T1/2 = ~ 39 h) and trypsin (T1/2 = ~ 32 min) half life, which is therapeutically remarkable feature. The cytotoxic activity of enzyme was examined against a panel of human cancer cell lines, HL-60, MOLT-4, MDA-MB-231 and T47D, and highest cytotoxicity observed against HL-60 cells (IC50 ~ 3.1 IU ml-1), which was comparable to commercial asparaginase. Cell and nuclear morphological studies of HL-60 cells showed that on treatment with purified asparaginase symptoms of apoptosis were increased in dose dependent manner. Cell cycle progression analysis indicates that enzyme induces apoptosis by cell cycle arrest in G0/G1 phase. Mitochondrial membrane potential loss showed that enzyme also triggers the mitochondrial pathway of apoptosis. Furthermore, the enzyme was found to be nontoxic for human noncancerous cells FR-2 and nonhemolytic for human erythrocytes.
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