Cloning and expression of the dihydroorotate dehydrogenase from Toxoplasma gondii.
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.
Sierra Pagan
Maria L
ML
Department of Biochemistry, University of Puerto Rico School of Medicine, Medical Sciences Campus, P.O. Box 365067, San Juan 00936-5067, Puerto Rico.
Zimmermann
Barbara H
BH
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D000090722:Dihydroorotate Dehydrogenase; D015723:Gene Library; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D016415:Sequence Alignment; D014122:Toxoplasma / Q000201:enzymology / Q000235:genetics*
D000090722:Dihydroorotate Dehydrogenase; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors