Parasitol Res. 2008 Feb 15 [Epub ahead of print]
Molecular and biochemical characterization of Toxoplasma gondii beta-hydroxyacyl-acyl carrier protein dehydratase (FABZ)
Dautu G, Ueno A, Munyaka B, Carmen G, Makino S, Kobayashi Y, Igarashi M.
National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, 2-13 Inada-cho, Obihiro, Hokkaido, 080-8555, Japan.
Toxoplasma gondii, unlike its mammalian host, utilizes a type II fatty acid biosynthesis pathway in which the steps of fatty acid biosynthesis are catalyzed by independent enzymes. Due to this difference, the enzymes of this pathway are good targets for the development of new therapeutic drugs directed against toxoplasmosis. In this report, we show by using reverse transcription-polymerase chain reaction analysis that beta-Hydroxyacyl-acyl carrier protein dehydratase (TgFABZ) is expressed both in tachyzoites and bradyzoites. Indirect immunofluorescence antibody test further shows the localization of TgFABZ protein in the apicoplast of both tachyzoites and bradyzoites. Enzyme dynamic analysis shows that the purified recombinant TgFABZ protein is soluble and active. The K(m) value of the enzyme for its substrate analog crotonoyl-CoA was estimated to be 82.57 +/- 10 muM.
PMID: 18274777 [PubMed - as supplied by publisher]