ArticleBioscience reports2015
Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- A universal polyphosphate kinase powers in vitro transcription.Nature communications · 2026Article
- Synthesis of 2'-fucosyllactose using multi-enzyme cascade with cofactor regeneration.Scientific reports · 2025Article
- Polyphosphate Kinase fromInternational journal of molecular sciences · 2024Article
- Engineering the thermal stability of a polyphosphate kinase by ancestral sequence reconstruction to expand the temperature boundary for an industrially applicable ATP regeneration system.Applied and environmental microbiology · 2024Article
- A Multi-enzyme Cascade for the Biosynthesis of AICA Ribonucleoside Di- and Triphosphate.Chembiochem : a European journal of chemical biology · 2022Article
- Polyphosphate Kinase 2 (PPK2) Enzymes: Structure, Function, and Roles in Bacterial Physiology and Virulence.International journal of molecular sciences · 2022Review
- In vitro biosynthesis of ATP from adenosine and polyphosphate.Bioresources and bioprocessing · 2021Article
- Article
- A Multi-Enzyme Cascade Reaction for the Production of 2'3'-cGAMP.Biomolecules · 2021Article
- A bicyclicRSC chemical biology · 2021Article
- Broad-Spectrum Inhibitor of Bacterial Polyphosphate Homeostasis Attenuates Virulence Factors and Helps Reveal Novel Physiology ofFrontiers in microbiology · 2021Article
- Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Polyphosphate Kinase Antagonizes Virulence Gene Expression in Francisella tularensis.Journal of bacteriology · 2018Article
- [Expression of Proteus mirabilis polyphosphate kinase and preparation of its polyclonal antibodies].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The metabolism of polyphosphate is important for the virulence of a wide range of pathogenic bacteria and the enzymes of polyphosphate metabolism have been proposed as an anti-bacterial target. In the intracellular pathogen Francisella tularensis, the product of the gene FTT1564 has been identified as a polyphosphate kinase from the polyphosphate kinase 2 (PPK2) family. The isogenic deletion mutant was defective for intracellular growth in macrophages and was attenuated in mice, indicating an important role for polyphosphate in the virulence of Francisella. Herein, we report the biochemical and structural characterization of F. tularensis polyphosphate kinase (FtPPK2) with a view to characterizing the enzyme as a novel target for inhibitors. Using an HPLC-based activity assay, the substrate specificity of FtPPK2 was found to include purine but not pyrimidine nts. The activity was also measured using (31)P-NMR. FtPPK2 has been crystallized and the structure determined to 2.23 Å (1 Å=0.1 nm) resolution. The structure consists of a six-stranded parallel β-sheet surrounded by 12 α-helices, with a high degree of similarity to other members of the PPK2 family and the thymidylate kinase superfamily. Residues proposed to be important for substrate binding and catalysis have been identified in the structure, including a lid-loop and the conserved Walker A and B motifs. The ΔFTT1564 strain showed significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic. This combination of biochemical, structural and microbiological data provide a sound foundation for future studies targeting the development of PPK2 small molecule inhibitors.
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