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From the
1 From the Lipid Metabolism Laboratory, Veterans Administration Hospital, and the Departments of Biochemistry and Physiological Chemistry, University of Wisconsin, Madison, Wisconsin 53706
Mevalonic kinase (EC 2.7.1.36), the first enzyme in the ATP-requiring sequence of cholesterol biosynthesis, has been purified from hog liver. This enzyme has a specific activity of 17 µmoles of product formed per min per mg of protein. The purified mevalonic kinase is homogeneous, or nearly homogeneous, on assay by Sephadex gel filtration, polyacrylamide gel electrophoresis, electrofocusing, and sucrose density gradient centrifugation. The molecular weight of this enzyme is estimated to be 98,000 from its elution position on Sephadex gel filtration. From a combination of studies on the initial velocity of the reaction, inhibition by product, and inhibition by dead end inhibitor, it is concluded that (a) the phosphorylation of mevalonic acid, catalyzed by mevalonic kinase, is sequential; that is, all substrates must react with the enzyme before the first product is released, (b) mevalonate reacts with the enzyme first, followed by MgATP, and (c) the order of release of products is first mevalonate 5-phosphate and then ADP. Evidence is also presented that an —SH group is important in the phosphorylation of mevalonic acid and that the reactivity of this group is influenced by the presence of potassium mevalonate and MgATP. No evidence has been obtained for the formation of enzyme-bound intermediates in this reaction.
Purification and Mechanism of Action of Hog Liver Mevalonic Kinase
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