Human liver sulphotransferase and UDP-glucuronosyltransferase: structure-activity relationship for phenolic substrates.
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.
Temellini
A
A
Department of Experimental Biomedicine, Medical School, University of Pisa, Italy.
Franchi
M
M
Giuliani
L
L
Pacifici
G M
GM
D000328:Adult; D005260:Female; D014453:Glucuronosyltransferase / Q000378:metabolism*; D006801:Humans; D062385:Hydroxybenzoates / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008875:Middle Aged; D015394:Molecular Structure; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D015238:Sulfotransferases / Q000378:metabolism*
D062385:Hydroxybenzoates; D010636:Phenols; D014453:Glucuronosyltransferase; D015238:Sulfotransferases