After removal of myrosinase activity by concanavalin A-Sepharose 4B chromatography, cell-free extracts of light-grown cress (Lepidium sativum L.) seedlings, catalyzed the sulfation of desulfobenzylglucosinolate (K(m), 0.23 millimolar) to benzylglucosinolate using PAPS (K(m), 1 millimolar) as sulfur donor. Sulfotransferase activity, which was optimal at pH 9.0, was stimulated by MgCl(2), MnCl(2), beta-mercaptoethanol, and dithiothreitol and was inhibited by ZnSO(4) and SH-reagents. The enzyme also sulfated desulfoallyglucosinolate to allylglucosinolate (sinigrin) but was inactive towards all phenylpropanoids and flavonoids tested.
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Glendening et al. (1988) studied this question.
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