The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases. - Archive ouverte HAL Access content directly
Journal Articles BMC Biochemistry Year : 2011

The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.

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Thiago Gastardelo
  • Function : Author
  • PersonId : 910965
Hugo de Almeida
  • Function : Author
  • PersonId : 910966
Izabela Bastos
  • Function : Author
  • PersonId : 910967
Raquel Negreiros
  • Function : Author
  • PersonId : 910968
Meire Lima
  • Function : Author
  • PersonId : 910969
Keyla Almeida
  • Function : Author
  • PersonId : 910971
Christine Ebel
Bergmann Ribeiro
  • Function : Author
  • PersonId : 910973
Carlos Felix
  • Function : Author
  • PersonId : 910974
Jaime Santana
  • Function : Correspondent author
  • PersonId : 910975

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Abstract

ABSTRACT: BACKGROUND: Pathogens 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. RESULTS: The 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 oC. Conversely, its recombinant form is thermophilic and requires alkaline pH. CONCLUSIONS: LAPTc 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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Dates and versions

inserm-00626328 , version 1 (25-09-2011)

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Gloria Cadavid-Restrepo, Thiago Gastardelo, Eric Faudry, Hugo de Almeida, Izabela Bastos, et al.. The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.. BMC Biochemistry, 2011, 12 (1), pp.46. ⟨10.1186/1471-2091-12-46⟩. ⟨inserm-00626328⟩
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