Cloning and expression of the dihydroorotate dehydrogenase from Toxoplasma gondii

• Published in: Biochimica et biophysica acta Vol. 1637; no. 2; pp. 178 - 181
• Main Authors: Sierra Pagan, Maria L, Zimmermann, Barbara H
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 20-03-2003
• Subjects: Amino Acid Sequence; Animals; Cloning, Molecular; Dihydroorotate dehydrogenase; Gene Library; Molecular Sequence Data; Oxidoreductases - biosynthesis; Oxidoreductases - chemistry; Oxidoreductases - genetics; Oxidoreductases Acting on CH-CH Group Donors; Pyrimidine biosynthesis; Sequence Alignment; Toxoplasma - enzymology; Toxoplasma - genetics; Toxoplasma gondii; Toxoplasma gondii; DHODase; Pyrimidine biosynthesis; Dihydroorotate dehydrogenase; PCR
• ISSN: 0925-4439; 0006-3002; 1879-260X
• DOI: 10.1016/S0925-4439(02)00226-0

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.