Sulfation, an important metabolic process in the human body, is an essential pathway through which endogenous catecholamine and xenobiotic substances can be inactivated and/or have their solubility increased to facilitate removal from the body. One family of enzymes that implement this sulfation, the sulfotransferases (SULTs), catalyze the transfer of a sulfuryl group (-SO<sub>3</sub><sup>-</sup>) from 3-phosphoadenosine-5-phosphosulfate to various substrate molecules. Of particular interest is SULT1A3 because, while it shares 93% amino acid sequence identity with SULT1A1, the two sulfotransferases demonstrate very unique substrate selectivity with SULT1A1 preferentially sulfating simple phenols and SULT1A3 preferentially sulfating catecholamines, such as dopamine. This study will focus on the synthesis of a library of dopaminergic compounds, with each having a different electron donating or withdrawing group at the 6-position. These analogues have been investigated both in silico and in vitro for their binding in SULT1A3 in an effort to determine the molecular basis for its substrate selectivity. The synthesis, computational, and enzymatic assay results will be discussed.

Synthesis of dopaminergic compounds for analysis in SULT1A3

251st National Meeting (2016)

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