ArticlePloS one2016
Biochemical Characterization of Glutamate Racemase-A New Candidate Drug Target against Burkholderia cenocepacia Infections.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Crystal structure and Hirshfeld surface analysis of (Acta crystallographica. Section E, Crystallographic communications · 2025Article
- A stereochemical journey around spirocyclic glutamic acid analogs.Organic & biomolecular chemistry · 2022Article
- Methodological tools to study species of the genus Burkholderia.Applied microbiology and biotechnology · 2021Review
- Synthesis, crystal structure and antibacterial studies of dihydropyrimidines and their regioselectively oxidized products.RSC advances · 2021Article
- Chemical, Metabolic, and Cellular Characterization of a FtsZ Inhibitor Effective AgainstFrontiers in microbiology · 2020Article
- Heterologous expression, purification and biochemical characterization of a glutamate racemase (MurI) fromPeerJ · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The greatest obstacle for the treatment of cystic fibrosis patients infected with the Burkholderia species is their intrinsic antibiotic resistance. For this reason, there is a need to develop new effective compounds. Glutamate racemase, an essential enzyme for the biosynthesis of the bacterial cell wall, is an excellent candidate target for the design of new antibacterial drugs. To this aim, we recombinantly produced and characterized glutamate racemase from Burkholderia cenocepacia J2315. From the screening of an in-house library of compounds, two Zn (II) and Mn (III) 1,3,5-triazapentadienate complexes were found to efficiently inhibit the glutamate racemase activity with IC50 values of 35.3 and 10.0 μM, respectively. Using multiple biochemical approaches, the metal complexes have been shown to affect the enzyme activity by binding to the enzyme-substrate complex and promoting the formation of an inhibited dimeric form of the enzyme. Our results corroborate the value of glutamate racemase as a good target for the development of novel inhibitors against Burkholderia.
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