First three-dimensional structure of Toxoplasma gondii thymidylate synthase-dihydrofolate reductase: insights for catalysis, interdomain interactions, and substrate channeling.

@article{Sharma2013FirstTS,
  title={First three-dimensional structure of Toxoplasma gondii thymidylate synthase-dihydrofolate reductase: insights for catalysis, interdomain interactions, and substrate channeling.},
  author={Hitesh Sharma and Mark J. Landau and Melissa A Vargo and Krasimir A. Spasov and Karen S. Anderson},
  journal={Biochemistry},
  year={2013},
  volume={52 41},
  pages={7305-7317}
}
Most species, such as humans, have monofunctional forms of thymidylate synthase (TS) and dihydrofolate reductase (DHFR) that are key folate metabolism enzymes making critical folate components required for DNA synthesis. In contrast, several parasitic protozoa, including Toxoplasma gondii , contain a unique bifunctional thymidylate synthase-dihydrofolate reductase (TS-DHFR) having the catalytic activities contained on a single polypeptide chain. The prevalence of T. gondii infections across the… CONTINUE READING
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