ArticleBMC biochemistry2011
The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.
Article in BMC biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- Synthesis and Evaluation of Peptoid-Based Compound Libraries as Inhibitors of Parasite Metallo-Aminopeptidases.ChemMedChem · 2026Article
- Aminopeptidase Inhibition in Drug-Resistant Plasmodium falciparum: Structural, Functional, and Pharmacological Rationale for Targeting PfA-M1 and PfA-M17.ChemMedChem · 2026Review
- Advances and challenges in the search for new treatments for Chagas disease.Memorias do Instituto Oswaldo Cruz · 2026Review
- Identification and Validation of Compounds TargetingACS infectious diseases · 2024Article
- Proteomic diversification of spermatostyles among six species of whirligig beetles.Molecular reproduction and development · 2024Article
- Identification of a potent and selective LAPTc inhibitor by RapidFire-Mass Spectrometry, with antichagasic activity.PLoS neglected tropical diseases · 2024Article
- Differential expression of peptidases in Strigomonas culicis wild-type and aposymbiotic strains: from proteomic data to proteolytic activity.Memorias do Instituto Oswaldo Cruz · 2024Article
- Expression, Characterisation, Homology Modelling and Molecular Docking of a Novel M17 Family Leucyl-Aminopeptidase fromInternational journal of molecular sciences · 2023Article
- Hallmarks of the relationship between host andFrontiers in cellular and infection microbiology · 2023Review
- Profilin is involved in G1 to S phase progression and mitotic spindle orientation during Leishmania donovani cell division cycle.PloS one · 2022Article
- KBE009: A Bestatin-Like Inhibitor of theLife (Basel, Switzerland) · 2021Article
- Structural and Functional Basis of Potent Inhibition of Leishmanial Leucine Aminopeptidase by Peptidomimetics.ACS omega · 2021Article
- Biological and Molecular Effects ofFrontiers in cellular and infection microbiology · 2021Article
- High-Level Expression in Escherichia coli, Purification and Kinetic Characterization of LAPTc, a Trypanosoma cruzi M17-Aminopeptidase.The protein journal · 2019Article
- The Uptake and Metabolism of Amino Acids, and Their Unique Role in the Biology of Pathogenic Trypanosomatids.Pathogens (Basel, Switzerland) · 2018Review
- M1 aminopeptidases as drug targets: broad applications or therapeutic niche?The FEBS journal · 2017Review
- A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei.PLoS pathogens · 2017Article
- The Activity of a Hexameric M17 Metallo-Aminopeptidase Is Associated With Survival ofFrontiers in microbiology · 2017Article
- Bestatin induces specific changes in Trypanosoma cruzi dipeptide pool.Antimicrobial agents and chemotherapy · 2015Article
- Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii.PloS one · 2015Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPathogens depend on peptidase activities to accomplish many physiological processes, including interaction with their hosts, highlighting parasitic peptidases as potential drug targets. In this study, a major leucyl aminopeptidolytic activity was identified in Trypanosoma cruzi, the aetiological agent of Chagas disease.
resultsThe enzyme was isolated from epimastigote forms of the parasite by a two-step chromatographic procedure and associated with a single 330-kDa homohexameric protein as determined by sedimentation velocity and light scattering experiments. Peptide mass fingerprinting identified the enzyme as the predicted T. cruzi aminopeptidase EAN97960. Molecular and enzymatic analysis indicated that this leucyl aminopeptidase of T. cruzi (LAPTc) belongs to the peptidase family M17 or leucyl aminopeptidase family. LAPTc has a strong dependence on neutral pH, is mesophilic and retains its oligomeric form up to 80°C. Conversely, its recombinant form is thermophilic and requires alkaline pH.
conclusionsLAPTc is a 330-kDa homohexameric metalloaminopeptidase expressed by all T. cruzi forms and mediates the major parasite leucyl aminopeptidolytic activity. Since biosynthetic pathways for essential amino acids, including leucine, are lacking in T. cruzi, LAPTc could have a function in nutritional supply.
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