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- W1545175065 abstract "Abstract When the β-hydroxy-β-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 β-hydroxy-β-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 β-hydroxy-β-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 β-hydroxy-β-methylglutaric acid could not be detected when the enzyme was incubated with substrates." @default.
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- W1545175065 date "1966-03-01" @default.
- W1545175065 modified "2023-09-28" @default.
- W1545175065 title "The Biosynthesis of β-Hydroxy-β-methylglutaryl Coenzyme A in Yeast" @default.
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- W1545175065 doi "https://doi.org/10.1016/s0021-9258(18)96822-5" @default.
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