ArticleCurrent microbiology2025
Exploring Escherichia coli EGY Type II L-Asparaginase Variant of Unique Glutaminase Activity: Cloning, Expression, Biochemical Characterization, and Molecular Docking Analysis.
Article in Current microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Microbial L-asparaginase II is a cornerstone biopharmaceutical drug for the effective treatment of leukemia and other blood cancers. However, the associated cellular resistance mechanisms in response to the treatment require effective management and necessitate searching and developing of better versions of the enzyme. Overall, the current study described a new E. coli type II L-ASNase variant of unique L-glutaminase co-activity that was cloned into pET28a ( +) vector and expressed in E. coli BL21(DE3) pLysS as a cytosolic protein with a molecular weight of 38.390 kDa. The recombinant E. coli L-ASNase was purified by affinity chromatography and showed high specific activity of 7179.5 U/mg. The purified enzyme exhibited enormous thermal stability and its affinity for L-asparagine (L-Asn) and L-glutamine (L-Gln) was in silico analyzed by molecular docking and experimentally verified which indicated relatively similar affinity. The purified E. coli L-ASNase demonstrated high dual activities toward L-Asn (Km and Vmax 0.627 mM and 385 µmol min
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