ArticleBioorganic & medicinal chemistry letters2011
Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymes.
Article in Bioorganic & medicinal chemistry letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Unraveling endophytic diversity in dioecious Siraitia grosvenorii: implications for mogroside production.Applied microbiology and biotechnology · 2024Article
- Development and Validation of a Sensitive, Specific and Reproducible UPLC-MS/MS Method for the Quantification of OJT007, A Novel Anti-Leishmanial Agent: Application to a Pharmacokinetic Study.International journal of environmental research and public health · 2021Article
- Genome-Scale Metabolic Modeling Reveals Metabolic Alterations of Multidrug-ResistantMicroorganisms · 2020Article
- Toward a structome of Acinetobacter baumannii drug targets.Protein science : a publication of the Protein Society · 2020Article
- Pre-Clinical Pharmacokinetics, Tissue Distribution and Physicochemical Studies of CLBQ14, a Novel Methionine Aminopeptidase Inhibitor for the Treatment of Infectious Diseases.Drug design, development and therapy · 2020Article
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- A simple, sensitive and reliable LC-MS/MS method for the determination of 7-bromo-5-chloroquinolin-8-ol (CLBQ14), a potent and selective inhibitor of methionine aminopeptidases: Application to pharmacokinetic studies.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018Article
- The identification of inhibitory compounds of Rickettsia prowazekii methionine aminopeptidase for antibacterial applications.Bioorganic & medicinal chemistry letters · 2018Article
- Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.Bioorganic & medicinal chemistry · 2017Article
- Advances in Bacterial Methionine Aminopeptidase Inhibition.Current topics in medicinal chemistry · 2016Review
- Biochemical characterization of recombinant methionine aminopeptidases (MAPs) from Mycobacterium tuberculosis H37Rv.Molecular and cellular biochemistry · 2012Article
- A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.Journal of bacteriology · 2012Article
- Methionine aminopeptidases: Potential therapeutic target for microsporidia and other microbes.The Journal of eukaryotic microbiologyReview
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Drug resistance in gram-negative bacteria, such as Acinetobacter baumannii, is emerging as a significant healthcare problem. New antibiotics with a novel mechanism of action are urgently needed to overcome the drug resistance. Methionine aminopeptidase (MetAP) carries out an essential cotranslational methionine excision in many bacteria and is a potential target to develop such novel antibiotics. Two putative MetAP genes were identified in A. baumannii genome, but whether they actually function as MetAP enzymes was not known. Therefore, we established an efficient E. coli expression system for their production as soluble and metal-free proteins for biochemical characterization. We demonstrated that both could carry out the metal-dependent catalysis and could be activated by divalent metal ions with the order Fe(II) ≈ Ni(II) > Co(II) > Mn(II) for both. By using a set of metalloform-selective inhibitors discovered on other MetAP enzymes, potency and metalloform selectivity on the A. baumannii MetAP proteins were observed. The similarity of their catalysis and inhibition to other MetAP enzymes confirmed that both may function as competent MetAP enzymes in A. baumannii and either or both may serve as the potential drug target.
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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.