ArticleThe Journal of biological chemistry2014
Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani.
Article in The Journal of biological chemistry, 2014. 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, 23 citations in OpenAlex.
- Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026Review
- Toad's survivability and soil microbiome alterations impacted via individual abundance.Biologia futura · 2025Article
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- Genomic Insight of Leishmania Parasite: In-Depth Review of Drug Resistance Mechanisms and Genetic Mutations.ACS omega · 2024Review
- Aldehyde-mediated inhibition of asparagine biosynthesis has implications for diabetes and alcoholism.Chemical science · 2024Article
- Differential gene expression provides leads to environmentally regulated soybean seed protein content.Frontiers in plant science · 2023Article
- Omics data integration facilitates target selection for new antiparasitic drugs against TriTryp infections.Frontiers in pharmacology · 2023Article
- Article
- A Nuclear Magnetic Resonance-Based Metabolomic Study to Identify Metabolite Differences between Iranian Isolates ofIranian journal of medical sciences · 2021Article
- L-Asparaginase of Leishmania donovani: Metabolic target and its role in Amphotericin B resistance.International journal for parasitology. Drugs and drug resistance · 2017Article
- Leishmania infantum Asparagine Synthetase A Is Dispensable for Parasites Survival and Infectivity.PLoS neglected tropical diseases · 2016Article
- Transcriptomic profiling of host-parasite interactions in the microsporidian Trachipleistophora hominis.BMC genomics · 2015Article
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
Asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA), and the other is asparagine synthetase B (AsnB) that uses glutamine or ammonia as a nitrogen source. In a previous investigation using sequence-based analysis, we had shown that Leishmania spp. possess asparagine-tRNA synthetase paralog asparagine synthetase A (LdASNA) that is ammonia-dependent. Here, we report the cloning, expression, and kinetic analysis of ASNA from Leishmania donovani. Interestingly, LdASNA was both ammonia- and glutamine-dependent. To study the physiological role of ASNA in Leishmania, gene deletion mutations were attempted via targeted gene replacement. Gene deletion of LdASNA showed a growth delay in mutants. However, chromosomal null mutants of LdASNA could not be obtained as the double transfectant mutants showed aneuploidy. These data suggest that LdASNA is essential for survival of the Leishmania parasite. LdASNA enzyme was recalcitrant toward crystallization so we instead crystallized and solved the atomic structure of its close homolog from Trypanosoma brucei (TbASNA) at 2.2 Å. A very significant conservation in active site residues is observed between TbASNA and Escherichia coli AsnA. It is evident that the absence of an LdASNA homolog from humans and its essentiality for the parasites make LdASNA a novel drug target.
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