ArticleThe Journal of biological chemistry2008
FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- Anti-Tuberculosis Potential of OJT008 against Active and Multi-Drug-Resistant Mycobacterium Tuberculosis: In Silico and In Vitro Inhibition of Methionine Aminopeptidase.International journal of molecular sciences · 2023Article
- Chemoproteomics Reveals Disruption of Metal Homeostasis and Metalloproteins by the Antibiotic Holomycin.ACS chemical biology · 2023Article
- The Development of the Bengamides as New Antibiotics against Drug-Resistant Bacteria.Marine drugs · 2022Review
- During Oxidative Stress the Clp Proteins ofJournal of bacteriology · 2020Article
- Chemically-defined lactose-based autoinduction medium for site-specific incorporation of non-canonical amino acids into proteins.RSC advances · 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
- The structure of RdDddP from Roseobacter denitrificans reveals that DMSP lyases in the DddP-family are metalloenzymes.PloS one · 2014Article
- Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells.Journal of medicinal chemistry · 2013Article
- A new pharmacological agent (AKB-4924) stabilizes hypoxia inducible factor-1 (HIF-1) and increases skin innate defenses against bacterial infection.Journal of molecular medicine (Berlin, Germany) · 2012Article
- Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.European journal of medicinal chemistry · 2012Article
- Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Advances in microbial physiology · 2012Review
- Article
- Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ion.Journal of inorganic biochemistry · 2012Article
- Synthesis and biological evaluation of salicylate-based compounds as a novel class of methionine aminopeptidase inhibitors.Bioorganic & medicinal chemistry letters · 2011Article
- Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.European journal of medicinal chemistry · 2011Article
- Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives.ChemMedChem · 2011Article
- Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymes.Bioorganic & medicinal chemistry letters · 2011Article
- The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Divalent metal ions play a critical role in the removal of N-terminal methionine from nascent proteins by methionine aminopeptidase (MetAP). Being an essential enzyme for bacteria, MetAP is an appealing target for the development of novel antibacterial drugs. Although purified enzyme can be activated by several divalent metal ions, the exact metal ion used by MetAP in cells is unknown. Many MetAP inhibitors are highly potent on purified enzyme, but they fail to show significant inhibition of bacterial growth. One possibility for the failure is a disparity of the metal used in activation of purified MetAP and the metal actually used by MetAP inside bacterial cells. Therefore, the challenge is to elucidate the physiologically relevant metal for MetAP and discover MetAP inhibitors that can effectively inhibit cellular MetAP. We have recently discovered MetAP inhibitors with selectivity toward different metalloforms of Escherichia coli MetAP, and with these unique inhibitors, we characterized their inhibition of MetAP enzyme activity in a cellular environment. We observed that only inhibitors that are selective for the Fe(II)-form of MetAP were potent in this assay. Further, we found that only these Fe(II)-form selective inhibitors showed significant inhibition of growth of five E. coli strains and two Bacillus strains. We confirmed their cellular target as MetAP by analysis of N-terminal processed and unprocessed recombinant glutathione S-transferase proteins. Therefore, we conclude that Fe(II) is the likely metal used by MetAP in E. coli and other bacterial cells.
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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.