Dopamine (DA) is a neurotransmitter that plays a critical role in the human body and is metabolized by enzymes such as catechol O-methyltransferases or cytosolic sulfotransferases (SULTs). SULTs catalyze the transfer of a sulfuryl from PAPS to endogenous compounds and xenobiotics, thus increasing the solubility of these compounds and/or regulating their excretion. Of particular interest is SULT1A3 in particular, which has a strong affinity for catecholamines, such as dopamine, yet a weaker affinity for simple phenolic compounds. Even though key residues in the active site are known, Glu and Asp, the molecular basis of this selectivity is not completely understood. Previously synthesized dopamine derivatives were examined in a SULT1A3 enzymatic assay to determine the enzyme’s affinity for analogues. Derivatives substituted at the 6-position with varying electron donating and withdrawing groups and others that had the amino-ethyl tail substituted for a nitrile tail were examined. Preliminary studies have shown that these DA derivatives are sulfated by SULT1A3. Kinetic parameters for each analogue were determined, and results were compared to computational results.

HPLC analysis of sulfation of dopamine derivatives by SULT1A3

253rd National Meeting (2017)

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