Isolation and molecular characterization of the shikimate dehydrogenase domain from the Toxoplasma gondii AROM complex
| Autor: | Gianni M Castiglione, James Peek, Thomas Shi, Dinesh Christendat |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Protein Conformation Shikimic Acid chemistry.chemical_compound Biosynthesis parasitic diseases Aromatic amino acids Shikimate pathway Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence chemistry.chemical_classification Shikimate dehydrogenase biology Genetic Variation Toxoplasma gondii biology.organism_classification Molecular biology Recombinant Proteins Alcohol Oxidoreductases Kinetics Metabolic pathway Enzyme chemistry Biochemistry Parasitology Oxidation-Reduction Toxoplasma NADP |
| Zdroj: | Molecular and Biochemical Parasitology. 194:16-19 |
| ISSN: | 0166-6851 |
| DOI: | 10.1016/j.molbiopara.2014.04.002 |
| Popis: | The apicomplexan parasite Toxoplasma gondii, the etiologic agent of toxoplasmosis, is estimated to infect 10-80% of different human populations. T. gondii encodes a large pentafunctional polypeptide known as the AROM complex which catalyzes five reactions in the shikimate pathway, a metabolic pathway required for the biosynthesis of the aromatic amino acids and a promising target for anti-parasitic agents. Here, we present the isolation, cloning and kinetic characterization of the shikimate dehydrogenase domain (TgSDH) from the T. gondii AROM complex. Recombinant TgSDH catalyzed the NADP(+)-dependent oxidation of shikimate in the absence of the remaining AROM domains and was sensitive to inhibition by a previously identified SDH inhibitor. Analysis of the TgSDH amino acid sequence revealed a number of novel insertions not found in SDH homologs from other organisms. Nevertheless, a three-dimensional structural model of TgSDH predicts a high level of conservation in the 'core' structure of the enzyme. |
| Databáze: | OpenAIRE |
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