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• W1996925955 abstract "The membrane-bound, biosynthetic dihydro-orotate oxidase of Escherichia coli K12 has been purified 400–800-fold. The molecular weight of the enzyme was found to be about 67 000. The spectrum of enzyme solutions in the visible light range shows no indication that flavins are present. The solubilized enzyme is stimulated by ammonium sulfate. When added together with Triton X-100, another stimulator of the E. coli enzyme, ammonium sulfate stimulates 58% more than would be expected for an additive effect. The particulate enzyme is stabilized to heating at 60 °C by its substrate and by orotate, the product of its reaction. The nature of dihydro-orotate oxidase binding on the membrane is inferred from: (1)|Solubilization data. Dihydro-orotate oxidase can be solubilized completely by Triton X-100 or by phospholipase A2 treatment followed by a shift of pH from 7.6 to 8.4. Only partial solubilization is attained by alkaline pH alone, or by phospholipase treatment plus high salt concentration or bovine serum albumin. Phospholipase-solubilized and purified enzyme tends to aggregate more than Triton X-100-solubilized enzyme. (2)|Arrhenius plots which are biphasic (transition at 19 °C) for particulate or Triton X-100-solubilized enzyme, straight for phospholipase-solubilized enzyme, and biphasic for the latter when activities are measured in the presence of Triton X-100. (3)|Experiments testing enzyme accessibility to trypsin action. These suggest that dihydro-orotate oxidase is located on the inner side of the cytoplasmic membrane." @default.
• W1996925955 created "2016-06-24" @default.
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• W1996925955 date "1974-10-01" @default.
• W1996925955 modified "2023-09-24" @default.
• W1996925955 title "Dihydro-orotate oxidase of Escherichia coli K12: Purification, properties, and relation to the cytoplasmic membrane" @default.
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• W1996925955 doi "https://doi.org/10.1016/0005-2744(74)90007-2" @default.
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