ArticleACS chemical biology2014
Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of Mycobacteria.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Thioquinazolinones as Antituberculosis Agents Targeting Phosphopantetheinyl Transferase.Journal of medicinal chemistry · 2025Article
- Functional and structural characterization of Stenotrophomonas maltophilia EntB, an unusual form of isochorismatase for siderophore synthesis.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Targeting Siderophore Biosynthesis to Thwart Microbial Growth.International journal of molecular sciences · 2025Review
- Transcriptomic characterization of recombinantApplied and environmental microbiology · 2024Article
- Redirecting raltitrexed from cancer cell thymidylate synthase toScience advances · 2024Article
- Unlocking Opportunities forACS infectious diseases · 2024Review
- Article
- Polyfluorinated salicylic acid analogs do not interfere with siderophore biosynthesis.Tuberculosis (Edinburgh, Scotland) · 2023Article
- In Vitro and In Vivo Inhibition of theJournal of medicinal chemistry · 2022Article
- Inhibition of Indigoidine Synthesis as a High-Throughput Colourimetric Screen for Antibiotics Targeting the EssentialPharmaceutics · 2021Article
- The quest for the holy grail: new antitubercular chemical entities, targets and strategies.Drug discovery today · 2020Review
- Opposing reactions in coenzyme A metabolism sensitizeScience (New York, N.Y.) · 2019Article
- Mass spectral determination of phosphopantetheinylation specificity for carrier proteins inFEBS open bio · 2016Article
- Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy.Biochimica et biophysica acta · 2015Review
- Synthesis and Pharmacokinetic Evaluation of Siderophore Biosynthesis Inhibitors for Mycobacterium tuberculosis.Journal of medicinal chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
4'-Phosphopantetheinyl transferases (PPTase) post-translationally modify carrier proteins with a phosphopantetheine moiety, an essential reaction in all three domains of life. In the bacterial genus Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors. We solved the X-ray crystal structures and biochemically characterized the Sfp-type PPTases from two of the most prevalent Mycobacterial pathogens, PptT of M. tuberculosis and MuPPT of M. ulcerans. Structural analyses reveal significant differences in cofactor binding and active site composition when compared to previously characterized Sfp-type PPTases. Functional analyses including the efficacy of Sfp-type PPTase-specific inhibitors also suggest that the Mycobacterial Sfp-type PPTases can serve as therapeutic targets against Mycobacterial infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.