Biochemistry, Biophysics, and Structural Biology Commons^™

The Role Of Zinc In Dihydroorotase, Pamela S. Gilchrist

Dissertations and Theses

Dihydroorotase (4,4—dihydroorotic acid amidolyase, EC 3.5.2.3.) 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.