ArticleScientific reports2016
Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 89 citations in OpenAlex.
- Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV.Biomolecules · 2025Article
- Isolation and Characterization of L-Asparaginase-Producing Bacteria from the Arabian-Persian Gulf Region: First Report onMarine drugs · 2025Article
- Recent advances in L-Asparaginase enzyme production and formulation development for acrylamide reduction during food processing.Food chemistry: X · 2025Review
- Optimizing recombinant production of L-asparaginase 1 from Saccharomyces cerevisiae using response surface methodology.Folia microbiologica · 2024Article
- Pyruvate metabolism dictates fibroblast sensitivity to GLS1 inhibition during fibrogenesis.JCI insight · 2024Article
- Nonclinical Evaluation of Single-MutantInternational journal of molecular sciences · 2024Article
- Enzyme Engineering Strategies for the Bioenhancement of L-Asparaginase Used as a Biopharmaceutical.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Characterization of a Type II L-Asparaginase from the HalotolerantLife (Basel, Switzerland) · 2023Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- Characterization of L-asparaginase from Streptomyces koyangensis SK4 with acrylamide-minimizing potential in potato chips.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Endophytic Fungi as a Promising Source of Anticancer L-Asparaginase: A Review.Current microbiology · 2023Review
- A new extracellular glutaminase and urease-free L-asparaginase from Meyerozyma guilliermondii.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems.Frontiers in pharmacology · 2023Review
- L-Asparaginase fromPharmaceuticals (Basel, Switzerland) · 2022Article
- Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.Pharmaceutics · 2022Review
- Fusarium sp. L-asparaginases: purification, characterization, and potential assessment as an antileukemic chemotherapeutic agent.Environmental science and pollution research international · 2022Article
- Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.Nature communications · 2021Article
- Sequencing and characterization of an L-asparaginase gene from a new species of Penicillium section Citrina isolated from Cerrado.Scientific reports · 2021Article
- Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives.Microorganisms · 2021Review
- Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.IUCrJ · 2021Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-asparaginase (L-ASNase) (EC 3.5.1.1) is an important enzyme for the treatment of acute lymphoblastic leukaemia. Currently, the enzyme is obtained from bacteria, Escherichia coli and Erwinia chrysanthemi. The bacterial enzymes family is subdivided in type I and type II; nevertheless, only type II have been employed in therapeutic proceedings. However, bacterial enzymes are susceptible to induce immune responses, leading to a high incidence of adverse effects compromising the effectiveness of the treatment. Therefore, alternative sources of L-ASNase may be useful to reduce toxicity and enhance efficacy. The yeast Saccharomyces cerevisiae has the ASP1 gene responsible for encoding L-asparaginase 1 (ScASNase1), an enzyme predicted as type II, like bacterial therapeutic isoforms, but it has been poorly studied. Here we characterised ScASNase1 using a recombinant enzyme purified by affinity chromatography. ScASNase1 has specific activity of 196.2 U/mg and allosteric behaviour, like type I enzymes, but with a low K
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