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- W2015434643 abstract "When dihydro-orotate dehydrogenase, a membrane-bound enzyme of Escherichia coli K12, is treated with the nonionic detergents Triton X-100 or Brij 35 it loses oxidase activity, but its activity (V) with the artificial electron acceptor dichloro-phenolindophenol (DCIP) is increased when measured the presence of the detergent. Triton X-100 does not modify that Km,app of the enzyme but it changes the inhibition by the product orotic acid from a mixed to a competitive type. Triton X-100 also solubilizes the enzyme to give a particle of markedly smaller size and lower density. The solubilized enzyme is stimulated by phosphatidylethanolamine and diphosphati-dylglycerol but not as much as by Triton X-100. Phospholipase A2 treatment results in loss of activity. The latter effect seems to be due partly to inhibition by fatty acids and partly to the loss of phospholipids. Triton X-100 restores activity." @default.
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- W2015434643 date "1973-04-01" @default.
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- W2015434643 title "Dihydro-orotate dehydrogenase of Escherichia coli K12: Effects of Triton X-100 and phospholipids" @default.
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- W2015434643 doi "https://doi.org/10.1016/0005-2744(73)90149-6" @default.
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