Human cytosolic sulfotransferases (SULTs) catalyze the transfer of a sulfate group (-SO<sub>3</sub><sup>-</sup>) from 3'-phosphoadenosine-5'-phosphosulfate to the hydroxyl group of an acceptor substrate. SULTs increase the water solubility of many endogenous substances and xenobiotic compounds, regulating their metabolism and aiding in excretion. Despite structural similarities, each sub-family sulfates distinct substrates. The SULT1A1 sub-family targets phenolic compounds, while SULT1A3 sulfates catecholamines. Reasons for such substrate specificity are poorly understood, although specificity may be regulated by an Asp residue in the active site of SULT1A3. To investigate the factors that influence SULT1A3’s substrate selectivity, dopamine analogues were synthesized with either a modified ethylamine tail moiety or with substituents at the 6-position of the molecule of varying sizes and degrees of electron withdrawing and donating capabilities. The design, synthesis and analysis of these analogues in an enzymatic assay will be discussed.

Design and synthesis of dopamine analogs for analysis in SULT1A3

249th National Meeting (2015)

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