ArticleFrontiers in microbiology2014
L,L-diaminopimelate aminotransferase (DapL): a putative target for the development of narrow-spectrum antibacterial compounds.
Article in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 20 citations in OpenAlex.
- Modulation of the human fecal metabolome - Effect of polyphenols depends on the BMI.Current research in food science · 2025Article
- The exceptional form and function of the giant bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Role of Antimicrobial Drug in the Development of Potential Therapeutics.Evidence-based complementary and alternative medicine : eCAM · 2022Review
- Thermostable D-amino acid decarboxylases derived from Thermotoga maritima diaminopimelate decarboxylase.Protein engineering, design & selection : PEDS · 2021Article
- Comparative Molecular Dynamics Simulations Provide Insight Into Antibiotic Interactions: A Case Study Using the Enzyme L,L-Diaminopimelate Aminotransferase (DapL).Frontiers in molecular biosciences · 2020Article
- ThePlant direct · 2019Article
- The Quest for Novel Antimicrobial Compounds: Emerging Trends in Research, Development, and Technologies.Antibiotics (Basel, Switzerland) · 2019Review
- Characterization of recombinant dihydrodipicolinate synthase from the bread wheat Triticum aestivum.Planta · 2018Article
- The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
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6 authors at 3 institutions in 4 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Despite the urgent need for sustained development of novel antibacterial compounds to combat the drastic rise in antibiotic resistant and emerging bacterial infections, only a few clinically relevant antibacterial drugs have been recently developed. One of the bottlenecks impeding the development of novel antibacterial compounds is the identification of new enzymatic targets. The nutritionally essential amino acid anabolic pathways, for example lysine biosynthesis, provide an opportunity to explore the development of antibacterial compounds, since human genomes do not possess the genes necessary to synthesize these amino acids de novo. The diaminopimelate (DAP)/lysine (lys) anabolic pathways are attractive targets for antibacterial development since the penultimate lys precursor meso-DAP (m-DAP) is a cross-linking amino acid in the peptidoglycan (PG) cell wall of most Gram-negative bacteria and lys plays a similar role in the PG of most Gram-positive bacteria, in addition to its role as one of the 20 proteogenic amino acids. The L,L-diaminopimelate aminotransferase (DapL) pathway was recently identified as a novel variant of the DAP/lys anabolic pathways. The DapL pathway has been identified in the pathogenic bacteria belonging to the genus; Chlamydia, Leptospira, and Treponema. The dapL gene has been identified in the genomes of 381 or approximately 13% of the 2771 bacteria that have been sequenced, annotated and reposited in the NCBI database, as of May 23, 2014. The narrow distribution of the DapL pathway in the bacterial domain provides an opportunity for the development and or discovery of narrow spectrum antibacterial compounds.
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