EC Number |
General Information |
Reference |
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2.8.2.15 | malfunction |
knockdown of SULT2B1 in Hepa1-6 cells induces cell-cycle arrest and apoptosis and suppresses tumorigenesis in vivo |
726332 |
2.8.2.15 | metabolism |
enzyme SULT1E1 cannot catalyze the sulfation of either of these two DELTA4-3-ketosteroids, whereas SULT2B1b exhibits weak activity toward only 4-androstene-3,17-dione (7.1 pmol/min/mg enzyme), but not progesterone. Thus, SULT2A1 may be the only major human SULT that is capable of sulfating DELTA4-3-ketosteroids, particularly 4-androstene-3,17-dione |
760621 |
2.8.2.15 | more |
modeling of the binding of hSULT2A1 with substrate 4-androstene-3,17-dione using the crystal structure of 3-ketosteroid-DELTA4-(5alpha)-dehydrogenase from Rhodococcus jostii RHA1 in complex with 4-androstene-3,17-dione (PDB ID 4AT2) and two crystal structures of human SULT2A1 in complex with DHEA and lithocholic acid (PDB IDs 1J99 and 3F3Y) as templates. The intact steroid nucleus is important for the binding of DELTA4-3-keto steroids by SULT2A1. Proposed mechanism of DELTA4-3-ketosteroid sulfation by SULT2A1, overview. Enzyme residues W77 and H99 are likely involved in the catalysis, possibly in the deprotonation of C-6. The sulfation of 4-androstene-3,17-dione might progress through the formation of a hydroxyl group which is a typical target for sulfation, it would require the isomerization of 4-androstene-3,17-dione from a keto form to an enol form |
760621 |
2.8.2.15 | physiological function |
expression of St2b2 is a trigger of epidermal cell differentiation by controlling cholesterol sulfate level in the cells |
706919 |
2.8.2.15 | physiological function |
isoform SULT2B1b interacts with cytoskeletal proteins via a proline/serine-rich C-terminus. Such an interaction allows the enzyme to move along microfilaments such as actin filaments, and catalyze the sulfation of hydroxysteroids at specific intracellular locations |
724959 |
2.8.2.15 | physiological function |
SULT2B1b expression promotes proliferation of hepatocellular carcinoma cells in vitro and in vivo, which may contribute to the progression of hepatocellular carcinoma |
726332 |
2.8.2.15 | physiological function |
the enzyme SULT2B1b promotes hepatocyte proliferation by inactivating oxysterol/LXR signaling |
723910 |