ArticleJournal of medicinal chemistry2010
Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase.
Article in Journal of medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Structural insights into N-terminal methionine cleavage by the human mitochondrial methionine aminopeptidase, MetAP1D.Scientific reports · 2023Article
- 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
- The Biotin Biosynthetic Pathway in Mycobacterium tuberculosis is a Validated Target for the Development of Antibacterial Agents.Current medicinal chemistry · 2020Review
- Self-derived structure-disrupting peptides targeting methionine aminopeptidase in pathogenic bacteria: a new strategy to generate antimicrobial peptides.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- Comparative analysis of homologous aminopeptidase PepN from pathogenic and non-pathogenic mycobacteria reveals divergent traits.PloS one · 2019Article
- 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
- Discovery of Inhibitors ofACS medicinal chemistry letters · 2013Article
- Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells.Journal of medicinal chemistry · 2013Article
- Structural analysis of bengamide derivatives as inhibitors of methionine aminopeptidases.Journal of medicinal chemistry · 2012Article
- Analogs of N'-hydroxy-N-(4H,5H-naphtho[1,2-d]thiazol-2-yl)methanimidamide inhibit Mycobacterium tuberculosis methionine aminopeptidases.Bioorganic & medicinal chemistry · 2012Article
- Biochemical characterization of recombinant methionine aminopeptidases (MAPs) from Mycobacterium tuberculosis H37Rv.Molecular and cellular biochemistry · 2012Article
- Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.European journal of medicinal chemistry · 2012Article
- Characterization of clioquinol and analogues as novel inhibitors of methionine aminopeptidases from Mycobacterium tuberculosis.Tuberculosis (Edinburgh, Scotland) · 2011Article
- Screening a fragment cocktail library using ultrafiltration.Analytical and bioanalytical chemistry · 2011Article
- Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.BMC biochemistry · 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
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Methionine aminopeptidase (MetAP) carries out an important cotranslational N-terminal methionine excision of nascent proteins and represents a potential target to develop antibacterial and antitubercular drugs. We cloned one of the two MetAPs in Mycobacterium tuberculosis (MtMetAP1c from the mapB gene) and purified it to homogeneity as an apoenzyme. Its activity required a divalent metal ion, and Co(II), Ni(II), Mn(II), and Fe(II) were among activators of the enzyme. Co(II) and Fe(II) had the tightest binding, while Ni(II) was the most efficient cofactor for the catalysis. MtMetAP1c was also functional in E. coli cells because a plasmid-expressed MtMetAP1c complemented the essential function of MetAP in E. coli and supported the cell growth. A set of potent MtMetAP1c inhibitors were identified, and they showed high selectivity toward the Fe(II)-form, the Mn(II)-form, or the Co(II) and Ni(II) forms of the enzyme, respectively. These metalloform selective inhibitors were used to assign the metalloform of the cellular MtMetAP1c. The fact that only the Fe(II)-form selective inhibitors inhibited the cellular MtMetAP1c activity and inhibited the MtMetAP1c-complemented cell growth suggests that Fe(II) is the native metal used by MtMetAP1c in an E. coli cellular environment. Finally, X-ray structures of MtMetAP1c in complex with three metalloform-selective inhibitors were analyzed, which showed different binding modes and different interactions with metal ions and active site residues.
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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.