17β-HSD14 Inhibitors

17β-HSD14 inhibitors are a distinctive class of compounds that do not directly target the enzyme's active site but modulate its activity by influencing the availability of substrates or cofactors required for its catalytic action. This modulation is achieved through various biochemical pathways and interactions with different cellular components.

Alizarin, for example, exerts its inhibitory effect by chelating zinc, a vital cofactor for 17β-HSD14, thus potentially altering the enzyme's conformation and function. Similarly, heavy metals like lead acetate and cadmium chloride disrupt enzyme activity by binding to thiol groups or replacing essential metal cofactors within the enzyme. Arsenic trioxide extends this approach by targeting sulfhydryl groups on proteins, which could inactivate 17β-HSD14.