Enzymatic Dehydration of 3-Hydroxymethyloxindole

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Abstract
Crude and partially purified extracts of wheat (Triticum vulgare, red variety) germ catalyze the dehydration of 3-hydroxymethyloxindole to 3-methyleneoxindole. Examination of the ultraviolet absorption spectrum of a reaction mixture consisting of either the extract or partially purified enzyme and 3-hydroxymethyloxindole, shows that this oxindole has undergone complete dehydration to 3-methyleneoxindole. TPNH-linked 3-methyleneoxindole reductase, also a constituent of the wheat germ extract, can be separated from the dehydrase by passage through an Agarose 15 column. Utilizing these partially purified enzymes, it can be demonstrated that the dehydrase activity found in wheat germ is a discrete enzymatic function.