ArticleNucleic acids research2006
Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding.
Article in Nucleic acids research, 2006. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Identification and characterization of RacX, a new broad-specificity amino acid racemase from a novel taxon within the orderApplied and environmental microbiology · 2026Article
- SuperbugCurrent topics in medicinal chemistry · 2025Article
- L-serine-O-sulfate alters cellular ultrastructure and mitigates the capacity of biofilm formation inCurrent research in microbial sciences · 2025Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Glutamate Racemase Is the Primary Target of β-Chloro-d-Alanine in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2016Article
- DNA Gyrase of Deinococcus radiodurans is characterized as Type II bacterial topoisomerase and its activity is differentially regulated by PprA in vitro.Extremophiles : life under extreme conditions · 2016Article
- Direct regulation of topoisomerase activity by a nucleoid-associated protein.Nucleic acids research · 2014Article
- Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Applied microbiology and biotechnology · 2011Review
- Glutamate racemase as a target for drug discovery.Microbial biotechnology · 2008Review
- YacG from Escherichia coli is a specific endogenous inhibitor of DNA gyrase.Nucleic acids research · 2008Article
- Cell-free protein synthesis of perdeuterated proteins for NMR studies.Journal of biomolecular NMR · 2007Article
- Functional comparison of the two Bacillus anthracis glutamate racemases.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate racemase (MurI) catalyses the conversion of l-glutamate to d-glutamate, an important component of the bacterial cell wall. MurI from Escherichia coli inhibits DNA gyrase in presence of the peptidoglycan precursor. Amongst the two-glutamate racemases found in Bacillus subtilis, only one inhibits gyrase, in absence of the precursor. Mycobacterium tuberculosis has a single gene encoding glutamate racemase. Action of M.tuberculosis MurI on DNA gyrase activity has been examined and its mode of action elucidated. We demonstrate that mycobacterial MurI inhibits DNA gyrase activity, in addition to its precursor independent racemization function. The inhibition is not species-specific as E.coli gyrase is also inhibited but is enzyme-specific as topoisomerase I activity remains unaltered. The mechanism of inhibition is different from other well-known gyrase inhibitors. MurI binds to GyrA subunit of the enzyme leading to a decrease in DNA-binding of the holoenzyme. The sequestration of the gyrase by MurI results in inhibition of all reactions catalysed by DNA gyrase. MurI is thus not a typical potent inhibitor of DNA gyrase and instead its role could be in modulation of the gyrase activity.
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