SULT2A7 Activators

Sulfotransferase family 2A, dehydroepiandrosterone (DHEA)-preferring, member 7 activators are compounds that influence the availability of its substrates or enhance the enzyme's catalytic efficiency. Flavonoids such as quercetin, chrysin, naringenin, and apigenin inhibit UGTs, enzymes that conjugate glucuronic acid to substrates, this inhibition can lead to higher levels of DHEA, the preferred substrate for Sult2a7. Enhanced levels of DHEA directly lead to increased enzymatic activity by providing more substrate for Sult2a7 to act upon. Piperine and curcumin, by inhibiting various drug-metabolizing enzymes, can also elevate the levels of endogenous substrates for Sult2a7, indirectly enhancing the enzyme's activity.

Magnesium and zinc serve as cofactors or structural stabilizers for enzymes, including sulfotransferases. Adequate levels of these minerals ensure that Sult2a7 has the necessary cofactors for its catalytic action, thus enhancing its activity. Selenium, by maintaining the structural integrity of enzymes, plays a role in ensuring the functional stability of Sult2a7. Sulforaphane may upregulate the expression or stabilize Sult2a7, which would result in enhanced sulfotransferase activity. Finally, caffeine, by inhibiting certain metabolic pathways, may lead to an increase in DHEA, boosting thefunctional activity of Sult2a7.