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Abstract Studies on the mechanism of the reversible enzymatic dehydration of d(-)-β-hydroxydecanoyl-N-acetylcysteamine to trans-2-decenoyl-N-acetylcysteamine and cis-3-decanoyl-N-acetylcysteamine are presented. They include determination of kinetic isotope effects with deuterium-labeled substrates and labeling experiments designed to follow the fates of the α- and γ-hydrogen atoms during the course of the reactions. The results show that trans-2-decenoyl-N-acetylcysteamine is formed directly by dehydration of β-hydroxydecanoate, whereas cis-3-decenoyl-N-acetylcysteamine arises only by isomerization of the conjugated enoate. The present findings, in conjunction with earlier kinetic data, lead to the conclusion that interconversion of the three substrates involves a common intermediate, presumably enzyme-bound α,β-decenoate.
Rando et al. (1968) studied this question.