ArticleScientific reports2022
Massive annotation of bacterial L-asparaginases reveals their puzzling distribution and frequent gene transfer events.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Unveiling a putative class 3 L-asparaginase in Glutamicibacter sp.: from soil isolation to in silico characterization.BMC biotechnology · 2026Article
- Stereochemical aspects of the nucleophilic attack in different classes of L-asparaginases.IUCrJ · 2026Review
- Optimizing Gene Sources for L-asparaginase Production: A Comparative Review.Current microbiology · 2025Review
- Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV.Biomolecules · 2025Article
- LM2I leads to CAD ubiquitination and liver cancer suppression through activation of ASS1.Acta biochimica et biophysica Sinica · 2025Article
- Exploring Escherichia coli EGY Type II L-Asparaginase Variant of Unique Glutaminase Activity: Cloning, Expression, Biochemical Characterization, and Molecular Docking Analysis.Current microbiology · 2025Article
- The structural insights of L-asparaginase from3 Biotech · 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
- Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV.Frontiers in chemistry · 2024Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli L-asparaginase EcAIII.Protein science : a publication of the Protein Society · 2023Article
- Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic Escherichia coli Ntn-amidohydrolase.Acta crystallographica. Section D, Structural biology · 2022Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-Asparaginases, which convert L-asparagine to L-aspartate and ammonia, come in five types, AI-AV. Some bacterial type AII enzymes are a key element in the treatment of acute lymphoblastic leukemia in children, but new L-asparaginases with better therapeutic properties are urgently needed. Here, we search publicly available bacterial genomes to annotate L-asparaginase proteins belonging to the five known types. We characterize taxonomic, phylogenetic, and genomic patterns of L-asparaginase occurrences pointing to frequent horizontal gene transfer (HGT) events, also occurring multiple times in the same recipient species. We show that the reference AV gene, encoding a protein originally found and structurally studied in Rhizobium etli, was acquired via HGT from Burkholderia. We also describe the sequence variability of the five L-asparaginase types and map the conservation levels on the experimental or predicted structures of the reference enzymes, finding the most conserved residues in the protein core near the active site, and the most variable ones on the protein surface. Additionally, we highlight the most common sequence features of bacterial AII proteins that may aid in selecting therapeutic L-asparaginases. Finally, we point to taxonomic units of bacteria that do not contain recognizable sequences of any of the known L-asparaginase types, implying that those microorganisms most likely contain new, as yet unknown types of L-asparaginases. Such novel enzymes, when properly identified and characterized, could hold promise as antileukemic drugs.
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