Inhibitors of Aspartate Transcarbamoylase Inhibit Mycobacterium tuberculosis Growth
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
37294060
DOI
10.1002/cmdc.202300279
Knihovny.cz E-zdroje
- Klíčová slova
- Mycobacterium tuberculosis, allosteric inhibition, aspartate transcarbamoylase, molecular docking, pyrimidine biosynthesis,
- MeSH
- Escherichia coli * MeSH
- kyselina asparagová MeSH
- lidé MeSH
- Mycobacterium tuberculosis * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kyselina asparagová MeSH
Aspartate transcarbamoylase (ATCase) plays a key role in the second step of de novo pyrimidine biosynthesis in eukaryotes and has been proposed to be a target to suppress cell proliferation in E. coli, human cells and the malarial parasite. We hypothesized that a library of ATCase inhibitors developed for malarial ATCase (PfATCase) may also contain inhibitors of the tubercular ATCase and provide a similar inhibition of cellular proliferation. Of the 70 compounds screened, 10 showed single-digit micromolar inhibition in an in vitro activity assay and were tested for their effect on M. tuberculosis cell growth in culture. The most promising compound demonstrated a MIC90 of 4 μM. A model of MtbATCase was generated using the experimental coordinates of PfATCase. In silico docking experiments showed this compound can occupy a similar allosteric pocket on MtbATCase to that seen on PfATCase, explaining the observed species selectivity seen for this compound series.
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