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The Biosynthesis of ß-Hydroxy-ß-methylglutaryl Coenzyme A in Yeast

IV. THE ORIGIN OF THE THIOESTER BOND OF -HYDROXY--METHYLGLUTARYL COENZYME A

From the ¹ From the Department of Biochemistry, Western Reserve University, School of Medicine, Cleveland, Ohio 44106

When the ß-hydroxy-ß-methylglutaryl coenzyme A-condensing enzyme system of yeast is incubated with unlabeled acetoacetyl coenzyme A and acetyl coenzyme A is labeled with ¹⁴C in the coenzyme A portion of the molecule, no radioactivity can be detected in ß-hydroxy-ß-methylglutaryl coenzyme A. When unlabeled acetyl coenzyme A and acetoacetyl coenzyme A labeled with tritium in the coenzyme A portion are the substrates, the resultant ß-hydroxy-ß-methylglutaryl coenzyme A retains the radioactivity. These results show that the thioester linkage of acetoacetyl coenzyme A remains intact during the condensation reaction. When the enzyme is incubated with [1-¹⁴C] acetyl coenzyme A, a protein-bound form of acetate can be isolated. Protein-bound ß-hydroxy-ß-methylglutaric acid could not be detected when the enzyme was incubated with substrates.

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