ArticleScientific reports2020
Generalized enzymatic mechanism of catalysis by tetrameric L-asparaginases from mesophilic bacteria.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- Enhanced production of extracellular L-asparaginase in batch culture via nitrous acid-induced mutagenesis of Aspergillus oryzae.Microbial cell factories · 2025Article
- Reversible Substrate-Specific Photocontrol of the Chemotherapeutic Asparaginase(-Glutaminase) fromACS catalysis · 2025Article
- Marine-derived L-asparaginase: unlocking marine power in anti-tumor therapeutics.Frontiers in immunology · 2025Review
- The structural insights of L-asparaginase from3 Biotech · 2024Article
- Towards a dependable data set of structures for L-asparaginase research.Acta crystallographica. Section D, Structural biology · 2024Article
- A Structural In Silico Analysis of the Immunogenicity of L-Asparaginase fromInternational journal of molecular sciences · 2024Article
- RrA, an enzyme from Rhodospirillum rubrum, is a prototype of a new family of short-chain L-asparaginases.Protein science : a publication of the Protein Society · 2024Article
- The dimeric form of bacterial l-asparaginase YpAI is fully active.The FEBS journal · 2023Article
- Article
- The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions.FEBS letters · 2022Article
- Recombinant production and characterization of L-glutaminase (glsA) as a promiscuity therapeutic enzyme.Applied microbiology and biotechnology · 2022Article
- L-Asparaginase fromPharmaceuticals (Basel, Switzerland) · 2022Article
- Structural Aspects ofInternational journal of molecular sciences · 2022Article
- Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.Pharmaceutics · 2022Review
- Revealing Escherichia coli type II L-asparaginase active site flexible loop in its open, ligand-free conformation.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
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5 authors at 2 institutions in 1 country.
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Abstract
The mechanism of catalysis by the L-glutaminase-asparaginase from Pseudomonas 7A (PGA) was investigated using structural, mass spectrometry, and kinetic data. We had previously proposed mechanism of hydrolysis of L-Asn by the type II L-asparaginase from E. coli (EcAII), but that work was limited to just one enzyme. Based on results presented in this report, we postulate that all homotetrameric L-asparaginases from mesophilic bacteria utilize a common ping-pong mechanism of catalysis consisting of two subsequent nucleophilic substitutions. Several new structures of non-covalent complexes of PGA with different substrates, as well as structures of covalent acyl-enzyme intermediates of PGA with canonical substrates (L-Asp and L-Glu) and an opportunistic ligand, a citrate anion, were determined. The results of kinetic experiments monitored by high-resolution LC/MS, when combined with new structural data, clearly show that the reaction catalyzed by L-glutaminase-asparaginases proceeds through formation of a covalent intermediate, as observed previously for EcAII. Additionally, by showing that the same mechanism applies to L-Asn and L-Gln, we postulate that it is common for all these structurally related enzymes.
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