ArticleInternational journal of molecular sciences2023
Enhancing the Catalytic Activity of Thermo-Asparaginase from
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 7 citations in OpenAlex.
- Hyperthermophilic L-Asparaginase fromInternational journal of molecular sciences · 2025Article
- Potential of Hyperthermophilic L-Asparaginase fromFoods (Basel, Switzerland) · 2025Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
L-asparaginases (L-ASNases) of microbial origin are the mainstay of blood cancer treatment. Numerous attempts have been performed for genetic improvement of the main properties of these enzymes. The substrate-binding Ser residue is highly conserved in L-ASNases regardless of their origin or type. However, the residues adjacent to the substrate-binding Ser differ between mesophilic and thermophilic L-ASNases. Based on our suggestion that the triad, including substrate-binding Ser, either GSQ for meso-ASNase or DST for thermo-ASNase, is tuned for efficient substrate binding, we constructed a double mutant of thermophilic L-ASNase from
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