Portland State University. Department of Biology
W. Herman Taylor
Date of Award
Master of Science (M.S.) in Biology
1 online resource (49 p.)
Dihydroorotase (4,4—dihydroorotic acid amidolyase, EC 220.127.116.11.) which catalyzes the reversible cyclization of N-carbamyl-L-aspartate to L-dihydroorotate has been purified from orotate-grown Clostridium oroticum. The enzyme is stable in 0.3 M sodium chloride and 10 µ ZnSO4. Sodium dodecyl sulfate gel electrophoresis indicates the enzyme to be composed of two identical subunits each with a molecular weight of 58,000 + 6000. Dihydroorotase is shown to be a zinc-containing metalloenzyme with 2 g atoms of zinc per 58,000 g of protein. The role of zinc in dihydroorotase is discussed.
Gilchrist, Pamela S., "The role of zinc in dihydroorotase" (1975). Dissertations and Theses. Paper 2015.