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Vol. 54, Issue 6, 942-948, December 1998
Department of Molecular and Cellular Pathology, University of
Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY,
Scotland, UK
Sulfation, catalyzed by members of the sulfotransferase (SULT)
superfamily, exerts considerable influence over the biological activity
of numerous endogenous and xenobiotic chemicals. In humans, catecholamines such as dopamine are extensively sulfated, and a SULT
isoform (SULT1A3 or the monoamine-sulfating form of
phenolsulfotransferase) has evolved with considerable
selectivity for dopamine and other biogenic amines. To investigate the
molecular basis for this selectivity, we identified a region of
SULT1A3, which, we hypothesized, contributes to its preference for
biogenic amines, and mutated two amino acids within this domain to the
corresponding residues in a closely related but functionally distinct
phenol sulfotransferase, SULT1A1 (H143Y and E146A). The change of a
single amino acid, E146A, was sufficient to transform the catalytic
properties and substrate preference of SULT1A3, such that they closely
resembled those of SULT1A1. These experiments confirm the functional
role of Glu146 in the selectivity of SULT1A3 for biogenic amines and
suggest that this region is a key determinant of sulfotransferase
substrate specificity.
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