Scymnol sulfotransferase

Scymnol sulfotransferase (EC 2.8.2.26) is a specialized enzyme primarily identified and characterized in the liver of cartilaginous fish, such as the dogfish shark (Squalus acanthias) (Macrides et al., 1994). Its principal biological role is the final step in the biosynthesis of scymnol sulfate, which serves as the primary bile salt in these species to facilitate the emulsification and absorption of dietary lipids (Pettigrew et al., 1998). The enzyme specifically targets the C-27 position of the bile alcohol scymnol, using 3-phosphoadenosine-5-phosphosulfate (PAPS) as the sulfate donor (Enzyme Nomenclature, EC 2.8.2.26). From an evolutionary perspective, scymnol sulfotransferase represents an ancestral mechanism of bile salt production that predates the evolution of C24 bile acids found in mammals (Kuroki et al., 2001). While scymnol itself has been investigated in pharmacological research for potential hepatoprotective and anti-inflammatory properties, the enzyme scymnol sulfotransferase is not currently recognized as a therapeutic target for human disease. In humans, the functional equivalent for sulfating steroids and bile acids is SULT2A1, but scymnol sulfotransferase remains a distinct biochemical entity specific to certain marine vertebrates (UniProtKB - P80102).

Other names

Scymnol 27-sulfotransferase3-alpha,7-alpha,12-alpha,24,26,27-hexahydroxy-5-beta-cholestane 27-sulfotransferaseAlcohol sulfotransferase (scymnol-specific)5-beta-cholestane-3-alpha,7-alpha,12-alpha,24,26,27-hexol 27-sulfotransferase

The enzyme catalyzes the transfer of a sulfate group from the donor molecule 3-phosphoadenosine-5-phosphosulfate (PAPS) to the C-27 hydroxyl group of the bile alcohol scymnol, resulting in the formation of scymnol sulfate and adenosine 3,5-bisphosphate.