Mw. Duffel, MOLECULAR SPECIFICITY OF ARYL SULFOTRANSFERASE-IV (TYROSINE-ESTER SULFOTRANSFERASE) FOR XENOBIOTIC SUBSTRATES AND INHIBITORS, Chemico-biological interactions, 92(1-3), 1994, pp. 3-14
Studies on the interactions of benzylic alcohols, aldehydes, and carbo
xylic acids with homogeneous preparations of aryl sulfotransferase (AS
T) IV have yielded information about the nature of the active site of
the enzyme. Lipophilicity and stereochemical configuration of benzylic
alcohols are key factors in determining their interaction with the ac
tive site of AST IV, Furthermore, aldehydes and carboxylic acids corre
sponding to the subsequent oxidation states derived from benzylic alco
hols are inhibitors of the enzyme. Additional investigations on the ca
talytic specificity of AST IV indicate that both primary and secondary
N-hydroxy arylamines can serve as substrates for the enzyme. These re
sults with benzylic alcohols, aldehydes, carboxylic acids, and N-hydro
xy arylamines have yielded insight into some of the parameters importa
nt in recognition of substrates and inhibitors by the active site of t
he enzyme and should be useful both in understanding in vivo metabolic
interactions and in designing appropriate new inhibitors to use as se
lective probes for the role of sulfation in metabolism of specific xen
obiotics.