Sulfation of mono- and diaryl oximes by aryl sulfotransferase isozymes.

Aryl sulfotransferases (3'-phosphoadenylsulfate:phenol sulfotransferase, EC 2.8.2.1) catalyze the sulfonation of a wide variety of hydroxyl-containing substrates, including numerous xenobiotics. The chemical diversity of aryl sulfotransferase substrates is in part attributable to the presence of multiple isozymes, each of which has broad substrate specificity. Of the aryl sulfotransferase isozymes in rat liver cytosol, two (designated isozymes I and II) have previously been shown to sulfonate phenolic compounds exclusively and, moreover, have very similar substrate specificity patterns. The recently reported unusually efficient, rapid isozyme I-catalyzed sulfonation of 9-fluorenone oxime (Mangold, J.B., Mangold, B.L.K. and Spina, A. (1986) Biochim. Biophys. Acta 874, 37-43) was therefore unexpected and suggested that aryl oximes may represent a useful class of model compounds to probe isozymic differences in substrate steric and electronic requirements. In the present study, several mono- and diaryl oximes have been prepared and tested as potential substrates for partially purified aryl sulfotransferases I and II from rat liver cytosol. The results indicate that steric factors, specifically planarity and hydroxyl group position, appear to be important requirements for enzyme-catalyzed sulfonation. In addition, although isozymes I and II had comparable activity with diaryl oximes, some striking differences in the ability of these two isozymes to sulfonate both substituted and unsubstituted monoaryl oximes were observed. This dissimilarity is consistent with distinct differences in the active sites of these isozymes.