EC Number   |
General Information |
Reference |
|---|
   2.8.2.14 | evolution |
full-length mL-STL cDNA has alternative exonic splicing variants and shares high amino acid sequence homology to the SULT2A family. The mL-STL gene belongs to the Sult2a family of a superfamily of cytosolic SULTs |
-, 761662 |
| 2.8.2.14 | malfunction |
substitutions of the two amino acids His48 and Leu99, which might have occurred during the evolution of the mouse SULT2A8 gene, endow mouse SULT2A8 the capacity to catalyze the 7-O-sulfation of bile acids |
760733 |
| 2.8.2.14 | malfunction |
tamoxifen or raloxifene are linked to the development of cholestasis, and inhibit sulfotransferase 2A1 (SULT2A1)-catalyzed dehydroepiandrosterone (DHEA) sulfonation |
761727 |
| 2.8.2.14 | more |
critical role of His48 in mouse cytosolic sulfotransferase SULT2A8 for the 7alpha-hydroxyl sulfation of bile acids. SULT2A8 lacks a conservative catalytic His residue at position 99th. Residues, His48 and Leu99 are unique to the mouse SULT2A8, but not other SULTs in general. They are essential for the enzyme's 7-O-sulfating activity toward bile acids and the strict substrate specificity toward 7alpha-hydroxyl bile acids |
760733 |
| 2.8.2.14 | physiological function |
members of the cytosolic sulfotransferase (SULT) SULT2A subfamily are known to be critically involved in the homeostasis of steroids and bile acids. SULT2A8, a 7alpha-hydroxyl bile acid-preferring mouse SULT, has been identified as the major enzyme responsible for the mouse-specific 7-O-sulfation of bile acids |
760733 |
| 2.8.2.14 | physiological function |
Sult2a8 is a major hepatic bile acid sulfonating enzyme in mice |
761661 |
| 2.8.2.14 | physiological function |
SULT2A8/mL-STL is a PPARalpha-regulated and 7alpha-hydroxylated bile acid-preferring cytosolic sulfotransferase, it is a liver-specific and male-dominant protein. PPARalpha modulates the homeostasis of bile acids during fasting being an essential regulator in bile acid biotransformation via sulfonation during fasting. The enzyme reveals a narrow sulfonating activity toward 7alpha-hydroxyl primary bile acids, including cholic acid, chenodeoxycholic acid, and alpha-muricholic acid, and thus may be the major hepatic bile acid sulfonating enzyme in mice |
-, 761662 |
