Cloned (Comment) | Organism |
---|---|
gene SULT1E1, localized to chromosome 4 (4q13.2), different transcripts and genetic variants, overview | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
V307I | polymorphism of SULT1E1 | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000029 | - |
17beta-estradiol | SULT1E1, pH and temperature not specified in the publication | Homo sapiens | |
0.00011 | - |
estrone | SULT1E1, pH and temperature not specified in the publication | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3'-phosphoadenylylsulfate + 17beta-estradiol | Homo sapiens | - |
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate | - |
? | |
3'-phosphoadenylylsulfate + estrone | Homo sapiens | - |
adenosine 3',5'-bisphosphate + estrone sulfate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P49888 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate | the proposed reaction mechanism: upon binding of PAPS, Ser137 forms an H-bond with Lys47, thus prevents its interaction with the bridging oxygenin PAPS and its further hydrolysis; His107 attracts a proton from the substrate hydroxyl (i.e. of E2 or DHEA), and enables nucleophilic attack at the sulfur atom in PAPS. In the next step, Lys47 interacts with the 5' phosphate of PAPS, which helps in dissociation of the sulfuryl group and in its transfer to the substrate. Finally, the reaction products, PAP and E1-S, are released, which completes the catalytic cycle | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
MCF-10A cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3'-phosphoadenylylsulfate + 17beta-estradiol | - |
Homo sapiens | adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate | - |
? | |
3'-phosphoadenylylsulfate + estrone | - |
Homo sapiens | adenosine 3',5'-bisphosphate + estrone sulfate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 35000, about, sequence calculation | Homo sapiens |
More | SULT1E1 is a dimer with an alpha/beta motif that consists of five parallel beta-strands surrounded by alpha-helices and a conserved alpha-helix across this structure | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
estrogen SULT | - |
Homo sapiens |
SULT1E1 | - |
Homo sapiens |
Organism | Comment | Expression |
---|---|---|
Homo sapiens | in liver SULT1E1 is repressed by xenobiotic activators of the pregnane X receptor and aryl hydrocarbon receptor peroxisome proliferator | down |
Homo sapiens | SULT1E1 is epigenetically regulated, as its expression is induced by the histone deacetylase inhibitor trichostatin A in MCF10A cells. In endometrial cancer cell line Ishikawa SULT1E1 is induced by steroid drug tibolone via progesterone receptor. In liver, it is activated via peroxisome proliferator activated receptor alpha and the liver X receptor | up |
General Information | Comment | Organism |
---|---|---|
metabolism | in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Further activation of estrone to the most potent estrogen, estradiol, is catalyzed by 17-ketosteroid reductases, while estradiol can also be formed from dehydroepiandrosterone by the sequential actions of 3beta-hydroxysteroid dehydrogenase-DELTA4-isomerase, aromatase, and 17-ketosteroid reductase. Roles of the STS and SULT enzymes in local estrogen biosynthesis, overview | Homo sapiens |
additional information | analysis of tertiary structure and reaction mechanism of the human SULT1E1 enzyme using the structure of the human SULT1E1 enzyme in complex with PAP and E2 (PDB ID 4JVL), catalytic amino acid residues His107, Lys47, and Ser137 play a role in the reaction mechanism | Homo sapiens |
physiological function | in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Enzyme SULT1E1 catalyzes the conjugation of estrone (E1) | Homo sapiens |