Human liver sulphotransferase and UDP-glucuronosyltransferase: Structure-activity relationship for phenolic substrates
- 1 January 1991
- journal article
- research article
- Published by Taylor & Francis in Xenobiotica
- Vol. 21 (2) , 171-177
- https://doi.org/10.3109/00498259109039459
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.Keywords
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