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Conjugation of a structurally diverse set of 53 catechol compounds was studied in vitro using six recombinant human sulfotransferases (SULTs), five UDP-glucuronosyltransferases (UGT) and the soluble form of catechol O-methyltransferase (S-COMT) as catalyst. The catechol set comprised endogenous compounds, such as catecholamines and catecholestrogens, drugs,(More)
Three-dimensional QSAR models were developed for predicting kinetic Michaelis constant (K(m)) values for phenolic substrates of human catecholamine sulfating sulfotransferase (SULT1A3). The K(m) values were correlated to the steric and electronic molecular fields of the substrates utilizing Comparative Molecular Field Analysis (CoMFA). The evaluated SULT1A3(More)
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