Brief communication: In silico identification of the protein disulfide isomerase family from a protozoan parasite

  • Authors:

  • Marco A. Ramos;Rosa E. Mares;Paloma D. Magaña;Joaquín E. Ortega;Jose M. Cornejo-Bravo

  • Affiliations:

  • Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico;Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico;Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico;Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico;Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico

  • Venue:
  • Computational Biology and Chemistry
  • Year:
  • 2008

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Abstract

Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze the correct formation of disulfide bonds during protein folding. Structurally they are characterized by the presence of functional thioredoxin-like (Trx) domains. For the protozoan parasite causative of the human amebiasis (Entamoeba histolytica), the correct formation of disulfide bonds is important for an accurate folding of its proteins, including some virulence factors. However, little is known about the enzymes involved in this mechanism. We undertook a post-genomic approach to identify the PDI family of this parasite. The genome database survey revealed a set of 11 PDI-encoding sequences with predictable protein thiol/disulfide oxidoreductase activities.