EC Number   |
General Information |
Reference |
|---|
    2.8.2.1 | evolution |
gene structure and genomic organization of each cynomolgus SULTs are similar to those of the human orthologues. Tissue distribution and sbstrate specificities of SULTS from humans and Cynomolgus macaques, overview |
760542 |
| 2.8.2.1 | metabolism |
isoform SULT4A1 interacts with both SULT1A1 and SULT1A3 when expressed in human cells. SULT4A1, SULT1A1, and SULT1A3 proteins form homodimers and heterodimers that require the sulfotransferase dimerization motif. A loss in SULT1A1/3 protein but an increase in SULT4A1 protein is observed during differentiation of neuronal SH-SY5Y cells, resulting in an increase in the toxicity of substrate dopamine |
760968 |
| 2.8.2.1 | metabolism |
no differences are found in in aristolochic acid I-/aristolochic acid II-DNA adduct levels wild-type mice and mice expressing human between isoforms SULT1A1/2 in all tissues analysed including kidney and liver. Sulfation by SULT1A1/2 is important in the activation of 3-nitrobenzanthrone |
760453 |
| 2.8.2.1 | metabolism |
of all thirteen known human SULTs, isoform SULT1A3 displays the strongest dextrorphan-sulfating activity |
760663 |
| 2.8.2.1 | metabolism |
relative quantification of sulfotransferases SULT1A1 and SULT1A3/4, intraday and interday variabilities are low in S9 and cell line matrices (below 8%) |
760969 |
| 2.8.2.1 | metabolism |
silencing of SULT1A1 and 3'-phosphoadenosine-5'-phosphosulfate synthase 2 leads to a significant decrease in aristolactam-DNA levels following exposure to aristolochic acid I. In GM00637 cells exposed to N-hydroxyaristolactam I, suppressing the sulfotransferase pathway leads to a significant decrease in aristolactam-DNA adduct formation |
760813 |
| 2.8.2.1 | metabolism |
sulfonation, catalyzed by PAPS-sulfotransferases, especially SULT2A1,is one major phase II pathways for polychlorobiphenylols conjugation and for elimination of the potentially toxic compounds, overview |
703487 |
