EC Number   |
General Information |
Reference |
|---|
   2.8.2.32 | evolution |
both Sult2st2 and Sult2st3 have evolved to sulfate specifically C27-bile alcohol, 5alpha-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlate with those of human SULT2A1. Whereas zebrafish Sult2 family members are active in the sulfation of bile alcohols, Sult3 family members sulfate 3beta-hydroxysteroids such as pregnenolone and DHEA |
761753 |
| 2.8.2.32 | evolution |
both Sult2st2 and Sult2st3 have evolved to sulfate specifically C27-bile alcohol, 5alpha-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlate with those of human SULT2A1. Whereas zebrafish Sult2 family members are active in the sulfation of bile alcohols, Sult3 family members sulfate 3beta-hydroxysteroids such as pregnenolone and DHEA. Substrate recognition sites of zebrafish Sult2 and Sult3 family members differ significantly from those of human SULT2A1 |
761753 |
| 2.8.2.32 | physiological function |
Sult2st2 and Sult2st3 are the major 5alpha-cyprinol-sulfating Sults in zebrafish that sulfate 5alpha-cyprinol at C27 position. Both Sult2st2 and Sult2st3 apparently do not distinguish between 5alpha-cyprinol and 5beta-cyprinol, two bile salts with opposite A/B ring junctions |
761753 |
