ArticleThe Journal of biological chemistry2014
Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 75 citations in OpenAlex.
- Overcoming challenges in the production of a human-like L-asparaginase: advanced strategies for expression and purification.Biotechnology reports (Amsterdam, Netherlands) · 2026Article
- Expression, Solubilization, and Refolding Recovery of a Novel l‑Asparaginase-Arginase 1 Chimera fromACS omega · 2026Article
- Characterization and bioactivities of glutaminase-free L-asparaginase from Salinicola acorporae S4-41.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
- Optimizing Gene Sources for L-asparaginase Production: A Comparative Review.Current microbiology · 2025Review
- Unveiling the Catalytic Mechanism and Conformational Dynamics of Guinea Pig l‑Asparaginase Type 1 for Leukemia Drug Design.ACS catalysis · 2025Article
- A mammalian, glutaminase-free asparaginase enhances venetoclax activity in preclinical AML models with chromosome 7 deletion.Frontiers in oncology · 2025Article
- Towards a dependable data set of structures for L-asparaginase research.Acta crystallographica. Section D, Structural biology · 2024Article
- TDP-43 proteinopathy in ALS is triggered by loss of ASRGL1 and associated with HML-2 expression.Nature communications · 2024Article
- Substrate Affinity Is Not Crucial for Therapeutic L-Asparaginases: Antileukemic Activity of Novel Bacterial Enzymes.Molecules (Basel, Switzerland) · 2024Article
- A Structural In Silico Analysis of the Immunogenicity of L-Asparaginase fromInternational journal of molecular sciences · 2024Article
- Elucidation of the Active Form and Reaction Mechanism in Human Asparaginase Type III Using Multiscale Simulations.Journal of chemical information and modeling · 2023Article
- In Silico Design of a Chimeric Humanized L-asparaginase.International journal of molecular sciences · 2023Article
- Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics.AMB Express · 2023Article
- Molecular cloning, characterization, and in-silico analysis of l-asparaginase from Himalayan3 Biotech · 2022Article
- Review
- Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.Pharmaceutics · 2022Review
- Novel Insights on the Use of L-Asparaginase as an Efficient and Safe Anti-Cancer Therapy.Cancers · 2022Review
- Highly Active Thermophilic L-Asparaginase fromInternational journal of molecular sciences · 2021Article
- Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.Nature communications · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The initial observation that guinea pig serum kills lymphoma cells marks the serendipitous discovery of a new class of anti-cancer agents. The serum cell killing factor was shown to be an enzyme with L-asparaginase (ASNase) activity. As a direct result of this observation, several bacterial L-asparaginases were developed and are currently approved by the Food and Drug Administration for the treatment of the subset of hematological malignancies that are dependent on the extracellular pool of the amino acid asparagine. As drugs, these enzymes act to hydrolyze asparagine to aspartate, thereby starving the cancer cells of this amino acid. Prior to the work presented here, the precise identity of this guinea pig enzyme has not been reported in the peer-reviewed literature. We discovered that the guinea pig enzyme annotated as H0W0T5_CAVPO, which we refer to as gpASNase1, has the required low Km property consistent with that possessed by the cell-killing guinea pig serum enzyme. Elucidation of the ligand-free and aspartate complex gpASNase1 crystal structures allows a direct comparison with the bacterial enzymes and serves to explain the lack of L-glutaminase activity in the guinea pig enzyme. The structures were also used to generate a homology model for the human homolog hASNase1 and to help explain its vastly different kinetic properties compared with gpASNase1, despite a 70% sequence identity. Given that the bacterial enzymes frequently present immunogenic and other toxic side effects, this work suggests that gpASNase1 could be a promising alternative to these bacterial enzymes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.