The porphyrin biosynthetic pathway in the malaria parasite has several unique features when compared to that of the human host. Heme, the end product of porphyrin metabolism in the malaria parasite, serves as an essential prosthetic group for the mitochondrial cytochromes that are involved in the electron transport chain. The enzymes of this pathway are localized in three different compartments, namely, mitochondrion, apicoplast, and cytosol. δ-Aminolevulinic acid (ALA), the committed precursor for heme, is synthesized in the parasite mitochondrion via Shemin pathway in which glycine and succinyl-CoA serve as precursors. The subsequent steps giving rise to coproporphyrinogen III take place in the apicoplast followed by the conversion of coproporphyrinogen III into protoporphyrinogen IX in the parasite cytosol....
KeywordsChlorophyll Malaria Cytosol Porphyrin Pyrrole
- Marks GS. Heme and chlorophyll: chemical, biochemical and medical aspects. London: D. Van Nostrand; 1969.Google Scholar
- Padmanaban G, Nagaraj VA, Rangarajan PN. Unique features of heme biosynthesis in the malaria parasite. In: Kadish KM, Smith KM, Guilard R, Ferreira GC, editors. Handbook of porphyrin science: with applications to chemistry, physics, materials science, engineering, biology and medicine. Hackensack: World Scientific; 2013;27:167–210.Google Scholar