Application | Comment | Organism |
---|---|---|
analysis | N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK, FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 can be used as an efficient fluorescent probe for the detection of Ox-LDL, LPC, and PAF, which could facilitate the mechanistic study, identification, diagnosis, prevention, and treatment of atherosclerosis | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Homo sapiens | 5829 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3'-phosphoadenylyl sulfate + estrone | Homo sapiens | - |
adenosine 3',5'-bisphosphate + estrone 3-sulfate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P49888 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
placenta | - |
Homo sapiens | - |
testis | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3'-phosphoadenylyl sulfate + estrone | - |
Homo sapiens | adenosine 3',5'-bisphosphate + estrone 3-sulfate | - |
? | |
additional information | human estrogen sulfotransferase and its related fluorescently labeled decapeptides with a YKDG sequence specifically interact with oxidized low-density lipoprotein. Interaction between human SULT1E1 (hSULT1E1), which has a YKEG sequence (residues 61-64) unlike other human SULTs, and Ox-LDL. hSULT1E1 specifically binds to Ox-LDL and its major lipid component (lysophosphatidylcholine, LPC), and platelet-activating factor (PAF), which bear a marked resemblance to LPC in terms of structure and activity. An N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK, FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 also specifically binds to Ox-LDL, LPC, and PAF | Homo sapiens | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | hSULT1E1 is biologically active as a dimer. hSULT1E1 may change its charge and structure in the presence of LDL/Ox-LDL, for example, a monomer or a dimer, likely leading to the change of biological activity of hSULT1E1 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
estrogen sulfotransferase | - |
Homo sapiens |
hSULT1E1 | - |
Homo sapiens |
SULT1E | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | hSULT1E1 may change its charge and structure in the presence of LDL/Ox-LDL, for example, a monomer or a dimer, likely leading to the change of biological activity of hSULT1E1 | Homo sapiens |
physiological function | estrogen sulfotransferase (SULT1E) mainly catalyzes the sulfation of estrogens, which are known to prevent the pathogenesis of atherosclerosis. Human estrogen sulfotransferase and its related fluorescently labeled decapeptides specifically interact with oxidized low-density lipoprotein, peptides with a YKDG sequence specifically bind to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis. Ox-LDL is abundant in atherosclerotic plaques and is associated with plaque instability. Ox-LDL is believed to cause cell formation in macrophages through Ox-LDL uptake via scavenger receptors in atherosclerotic lesions | Homo sapiens |