Functional characterization of the acyl carrier protein (PfACP) and beta-ketoacyl ACP synthase III (PfKASIII) from Plasmodium falciparum
| Autor: | Zhiyu Li, Patrice Sellers, Sean T. Prigge, Jill T Ferlan, Malcolm J. Gardner, Shamira J. Shallom, Norman C. Waters, Cassandra L. Woodard, Lan Wei, Karen M. Kopydlowski, Patricia J. Lee, Tadeusz Guszczynski |
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| Rok vydání: | 2002 |
| Předmět: |
Coenzyme A
Molecular Sequence Data Plasmodium falciparum Cofactor Serine chemistry.chemical_compound parasitic diseases 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase Acyl Carrier Protein Animals Amino Acid Sequence Cloning Molecular Molecular Biology Alanine chemistry.chemical_classification biology Fatty Acids Fatty acid biology.organism_classification Recombinant Proteins Acyl carrier protein Enzyme chemistry Biochemistry Amino Acid Substitution Mutation Pantetheine biology.protein Parasitology Fatty Acid Synthases Holoenzymes Sequence Alignment |
| Zdroj: | Molecular and biochemical parasitology. 123(2) |
| ISSN: | 0166-6851 |
| Popis: | The genome of the malaria parasite, Plasmodium falciparum, appears to contain the proteins necessary for a Type II dissociated fatty acid biosynthetic system. Here we report the functional characterization of two proteins from this system. Purified recombinant acyl carrier protein (ACP) and beta-ketoacyl-ACP synthase III (KASIII) from P. falciparum are soluble and active in a truncated form. Malarial ACP is activated by the addition of a 4'-phosphopantetheine prosthetic group derived from coenzyme A, generating holo-PfACP. Holo-PfACP is an effective substrate for the transacylase activity of PfKASIII, but substitution of a key active site cysteine in PfKASIII to alanine or serine abolishes enzymatic activity. During the schizont stage of parasite development, there is a significant up-regulation of the mRNAs corresponding to these proteins, indicating an important metabolic requirement for fatty acids during this stage. |
| Databáze: | OpenAIRE |
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