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In this study, researchers found that both thermolabile and thermostable forms of phenol sulfotransferase contribute to the sulfation of minoxidil, emphasizing the need to consider both enzymes in assessing sulfation in human tissues.

This study found that minoxidil is bioactivated through sulfation by the phenol-sulfating form of phenol sulfotransferase in human liver.

This review discusses recent molecular biology advances in the human phenol sulfotransferase gene family and reports no new results; the authors highlight its relevance for studies of endogenous and xenobiotic metabolism.

This study found that human liver dehydroepiandrosterone sulfotransferase (DHEA ST) catalyzes the sulfate conjugation of minoxidil, indicating another pathway contributing to its metabolism in humans.

This study found that at least four different human sulfotransferase activities contribute to the sulfation of minoxidil, complicating predictions of individual responses based on ST levels.