Previous studies had demonstrated that sulfation constituted a major pathway for the metabolism of
phenylephrine in vivo. The current study was designed to identify the major human SULT(s) responsible for the sulfation
of phenylephrine. Of the twelve human SULTs analyzed, SULT1A3 displayed the strongest sulfating activity toward
phenylephrine. The enzyme exhibited a pH optimum spanning 7 – 10.5. Kinetic analysis revealed that SULT1A3-
mediated sulfation of phenylephrine occurred in the same order of magnitude compared with that previously reported for
SULT1A3-mediated sulfation of dopamine. Moreover, sulfation of phenylephrine was shown to occur in HepG2 cells
under metabolic setting. Collectively, these results provided useful information concerning the biochemical basis
underlying the metabolism of phenylephrine in vivo as previously reported.
Keywords: Cytosolic sulfotransferase, phenylephrine, sulfation, SULT, SULT1A3.
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