Abstract
The substrate binding order of chicken liver mevalonate 5-diphosphate decarboxylase was investigated by using competitive inhibitors of the substrates. Mevalonate and mevalonate 5-phosphate showed mixed inhibition when ATP was the varied substrate. Both analogues of ATP, adenosine 5′- O-(3-thiotriphosphate) and β-τ methylene adenosine 5′-triphosphate showed uncompetitive inhibition against mevalonate 5-diphosphate. These results are in accordance with an ordered sequential mechanism with mevalonate 5-diphosphate as the first substrate to bind to the enzyme.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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