4.7 Article

Cloning and expression of the dihydroorotate dehydrogenase from Toxoplasma gondii

Journal

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S0925-4439(02)00226-0

Keywords

dihydroorotate dehydrogenase; Toxoplasma gondii; pyrimidine biosynthesis

Funding

  1. NCRR NIH HHS [G12RR-03051] Funding Source: Medline
  2. NIGMS NIH HHS [S06GM08824] Funding Source: Medline

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A full-length dihydroorotate dehydrogenase (DHODase) sequence was cloned from a Toxoplasma gondii tachyzoite cDNA library. The sequence was most similar to family 2 DHODases, and had a calculated molecular mass of 65.1 kDa. The full-length and two N-terminally truncated T. gondii DHODase sequences were expressed as recombinant proteins. One of the truncated sequences complemented a DHODase-deficient bacterial host. (C) 2002 Elsevier Science B.V. All rights reserved.

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