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Human liver sulphotransferase and UDP-glucuronosyltransferase: structure-activity relationship for phenolic
A Temellini1, M Franchi, L Giuliani
1Department of Experimental Biomedicine, Medical School, University of Pisa, Italy.
Xenobiotica; the Fate of Foreign Compounds in Biological Systems
|February 1, 1991
Abstract:
1. Human liver sulphotransferase and UDP-glucuronosyltransferase were studied with phenol, methyl-, ethyl-, propyl-, butyl-, phenyl-, nitro-, amino-phenols and hydroxybenzoic acids as substrates. 2. The Michaelis-Menten constants (Km) and the maximum velocities of reaction (Vmax) of sulphotransferase and UDP-glucuronosyltransferase for each substrate were measured. 3. The Km values for sulphotransferase varied over 5000-fold whereas they varied over 25-fold for UDP-glucuronosyltransferase. 4. Sulphotransferase and UDP-glucuronosyltransferase have different structure-activity relationships with phenolic substrates.