Abstract β-Hydroxy-β-methylglutaryl coenzyme A and the hemithioacetal addition compound of mevaldic acid and CoA were separately reduced by either Form A or B of [3H]NADPH in the presence of a partially purified β-hydroxy-β-methylglutaryl-CoA reductase obtained from yeast. Tritium was incorporated into product, mevalonic acid, in high yield from Form A of [3H]NADPH in each of these reactions. Only a trace of radioactivity was associated with mevalonic acid when the reduction was carried out under identical conditions with Form B of [3H]NADPH. Therefore, hydrogen is transferred from the A side of the pyridine ring of NADPH in each of these dehydrogenase-catalyzed reductions (ester (NADPH)/→ aldehyde-derivative (intermediate) (NADPH)/→ alcohol).
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Dugan et al. (1971) studied this question.
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