ArticlePloS one2012
Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 87 citations in OpenAlex.
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- Chemical probes for enzyme imaging: challenges in design, synthesis and biomedical applications.Chemical science · 2025Review
- Chemoproteomics validates selective targeting ofeLife · 2024Article
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- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Genetic and chemical validation ofeLife · 2022Article
- Peptidyl-Resin Substrates as a Tool in the Analysis of Caspase Activity.Molecules (Basel, Switzerland) · 2022Article
- Overexpression ofPathogens (Basel, Switzerland) · 2021Article
- KBE009: A Bestatin-Like Inhibitor of theLife (Basel, Switzerland) · 2021Article
- Mapping the substrate specificity of the Plasmodium M1 and M17 aminopeptidases.The Biochemical journal · 2021Article
- Identification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe.Molecular and biochemical parasitology · 2021Article
- Biochemical and cellular characterisation of the Plasmodium falciparum M1 alanyl aminopeptidase (PfM1AAP) and M17 leucyl aminopeptidase (PfM17LAP).Scientific reports · 2021Article
- Methods Used to Investigate theFrontiers in cellular and infection microbiology · 2021Review
- Driving antimalarial design through understanding of target mechanism.Biochemical Society transactions · 2020Review
- X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2.The Biochemical journal · 2020Article
- Localization and enzyme kinetics of aminopeptidase N3 from Toxoplasma gondii.Parasitology research · 2020Article
- Structural characterization of plasmodial aminopeptidase: a combined molecular docking and QSAR-based in silico approaches.Molecular diversity · 2019Article
- Characterization of P. falciparum dipeptidyl aminopeptidase 3 specificity identifies differences in amino acid preferences between peptide-based substrates and covalent inhibitors.The FEBS journal · 2019Article
- Fitness Loss under Amino Acid Starvation in Artemisinin-Resistant Plasmodium falciparum Isolates from Cambodia.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
10 authors at 7 institutions in 4 countries.
Funding
Abstract
backgroundPlasmodium falciparum, the causative agent of human malaria, expresses two aminopeptidases, PfM1AAP and PfM17LAP, critical to generating a free amino acid pool used by the intraerythrocytic stage of the parasite for proteins synthesis, growth and development. These exopeptidases are potential targets for the development of a new class of anti-malaria drugs. METHODOLOGY/PRINCIPAL
findingsTo define the substrate specificity of recombinant forms of these two malaria aminopeptidases we used a new library consisting of 61 fluorogenic substrates derived both from natural and unnatural amino acids. We obtained a detailed substrate fingerprint for recombinant forms of the enzymes revealing that PfM1AAP exhibits a very broad substrate tolerance, capable of efficiently hydrolyzing neutral and basic amino acids, while PfM17LAP has narrower substrate specificity and preferentially cleaves bulky, hydrophobic amino acids. The substrate library was also exploited to profile the activity of the native aminopeptidases in soluble cell lysates of P. falciparum malaria. CONCLUSIONS/SIGNIFICANCE: This data showed that PfM1AAP and PfM17LAP are responsible for majority of the aminopeptidase activity in these extracts. These studies provide specific substrate and mechanistic information important for understanding the function of these aminopeptidases and could be exploited in the design of new inhibitors to specifically target these for anti-malaria treatment.
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