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The novel heme oxygenase‐like protein from Plasmodium falciparum converts heme to bilirubin IXα in the apicoplast
Author(s) -
Okada Ken
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.12.015
Subject(s) - apicoplast , heme , plasmodium falciparum , heme oxygenase , biochemistry , bilirubin , biology , chemistry , malaria , enzyme , apicomplexa , immunology , endocrinology
The metabolic pathways in apicoplasts of human malaria parasites are promising drug targets. The apicomplexan parasites exhibit delayed cell death when their apicoplast is impaired, but the metabolic pathways within apicoplasts are poorly understood. A nuclear‐encoded heme oxygenase (HO)‐like protein with an apicoplast‐targeted bipartite transit peptide was identified in the Plasmodium falciparum genome. Purified mature recombinant PfHO protein converted heme into bilirubin IXα as confirmed by high‐performance liquid chromatography. In addition, PfHO required an iron chelator such as deferoxamine for complete activity. These observations lead to the conclusion that a novel enzymatic heme degradation system is present in human malaria parasites.