ArticleThe Biochemical journal2007
Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 48 citations in OpenAlex.
- Extracellular Vesicles in Bacteria, Archaea, and Eukaryotes: Mechanisms of Inter-Kingdom Communication and Clinical Implications.Microorganisms · 2025Review
- Nickel: Human Health and Environmental Toxicology.International journal of environmental research and public health · 2020Review
- The complete genome sequence of the thermophilic bacterium Laceyella sacchari FBKL4.010 reveals the basis for tetramethylpyrazine biosynthesis in Moutai-flavor Daqu.MicrobiologyOpen · 2019Article
- Potent and selective inhibitors for M32 metallocarboxypeptidases identified from high-throughput screening of anti-kinetoplastid chemical boxes.PLoS neglected tropical diseases · 2019Article
- Archaea Symbiont ofFrontiers in cellular and infection microbiology · 2018Article
- Genome evolution in trypanosomatid parasites.Parasitology · 2015Review
- Identification of differentially expressed proteins from Leishmania amazonensis associated with the loss of virulence of the parasites.PLoS neglected tropical diseases · 2014Article
- Characterization of the transcriptome and temperature-induced differential gene expression in QPX, the thraustochytrid parasite of hard clams.BMC genomics · 2014Article
- Characterization of the M32 metallocarboxypeptidase of Trypanosoma brucei: differences and similarities with its orthologue in Trypanosoma cruzi.Molecular and biochemical parasitology · 2012Article
- A global comparison of the human and T. brucei degradomes gives insights about possible parasite drug targets.PLoS neglected tropical diseases · 2012Article
- Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli.Molecular microbiology · 2011Article
- Mechanisms of nickel toxicity in microorganisms.Metallomics : integrated biometal science · 2011Review
- The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.BMC biochemistry · 2011Article
- Serine protease activities in Leishmania (Leishmania) chagasi promastigotes.Parasitology research · 2010Article
- Exocytosis and protein secretion in Trypanosoma.BMC microbiology · 2010Article
- Excreted/secreted proteins from trypanosome procyclic strains.Journal of biomedicine & biotechnology · 2010Article
- Development of protease inhibitors for protozoan infections.Current opinion in infectious diseases · 2008Review
- A proposed role for Leishmania major carboxypeptidase in peptide catabolism.Biochemical and biophysical research communications · 2008Article
- Unusual phyletic distribution of peptidases as a tool for identifying potential drug targets.The Biochemical journal · 2007Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
MCPs (metallocarboxypeptidases) of the M32 family of peptidases have been identified in a number of prokaryotic organisms, and only a few of them have been characterized biochemically. Members of this family are absent from eukaryotic genomes, with the remarkable exception of those of trypanosomatids. The genome of the CL Brener clone of Trypanosoma cruzi, the causative agent of Chagas' disease, encodes two such MCPs, with 64% identity between them: TcMCP-1 and TcMCP-2. Both genes, which are present in a single copy per haploid genome, were expressed in Escherichia coli as catalytically active polyHis-tagged recombinant enzymes. Despite their identity, the purified TcMCPs displayed marked biochemical differences. TcMCP-1 acted optimally at pH 6.2 on FA {N-(3-[2-furyl]acryloyl)}-Ala-Lys with a K(m) of 166 muM. Activity against benzyloxycarbonyl-Ala-Xaa substrates revealed a P1' preference for basic C-terminal residues. In contrast, TcMCP-2 preferred aromatic and aliphatic residues at this position. The K(m) value for FA-Phe-Phe at pH 7.6 was 24 muM. Therefore the specificities of both MCPs are complementary. Western blot analysis revealed a different pattern of expression for both enzymes: whereas TcMCP-1 is present in all life cycle stages of T. cruzi, TcMCP-2 is mainly expressed in the stages that occur in the invertebrate host. Indirect immunofluorescence experiments suggest that both proteins are localized in the parasite cytosol. Members of this family have been identified in other trypanosomatids, which so far are the only group of eukaryotes encoding M32 MCPs. This fact makes these enzymes an attractive potential target for drug development against these organisms.
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