EC Number | Application | Comment | Organism |
---|---|---|---|
2.8.2.2 | synthesis | cytosolic sulfotransferases (SULTs) acting as phase II metabolic enzymes can be used in the sulfonation of small molecules by transferring a sulfonate group from the unique co-factor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the substrates | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.8.2.2 | raloxifene | - |
Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.8.2.2 | cytosol | - |
Homo sapiens | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.2.2 | 3'-phosphoadenylyl sulfate + androsterone | Homo sapiens | - |
adenosine 3',5'-bisphosphate + androsterone 3-sulfate | - |
? | |
2.8.2.2 | 3'-phosphoadenylyl sulfate + dehydroepiandrosterone | Homo sapiens | - |
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.2.2 | Homo sapiens | Q06520 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.2.2 | 3'-phosphoadenylyl sulfate + androsterone | - |
Homo sapiens | adenosine 3',5'-bisphosphate + androsterone 3-sulfate | - |
? | |
2.8.2.2 | 3'-phosphoadenylyl sulfate + dehydroepiandrosterone | - |
Homo sapiens | adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate | - |
? | |
2.8.2.2 | 3'-phosphoadenylyl sulfate + lithocholic acid | substrate complex structure analysis | Homo sapiens | adenosine 3',5'-bisphosphate + lithocholate 3-sulfate | - |
? | |
2.8.2.2 | 3'-phosphoadenylyl sulfate + raloxifene | substrate complex structure analysis | Homo sapiens | adenosine 3',5'-bisphosphate + ? | - |
? | |
2.8.2.2 | additional information | cytosolic sulfotransferases (SULTs) can catalyze the sulfonation of small molecules by transferring a sulfonate group from the unique cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the substrates | Homo sapiens | ? | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.8.2.2 | HST | UniProt | Homo sapiens |
2.8.2.2 | hSULT2A1 | - |
Homo sapiens |
2.8.2.2 | hydroxysteroid | UniProt | Homo sapiens |
2.8.2.2 | sulfotransferase 2A1 | - |
Homo sapiens |
2.8.2.2 | SULT2A1 | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.8.2.2 | evolution | human cytosolic sulfotransferases (hSULTs) canbe classified into four families (hSULT1, hSULT2, hSULT4, and hSULT6) based on sequence similarity | Homo sapiens |
2.8.2.2 | additional information | mechanism for the effect of cofactor (PAP) and ligands (LCA, raloxifene, alpha-hydroxytamoxifen, ouabain, and 3'-phosphoadenylyl sulfate) on structural stability and selectivity of SULT2A1 from the perspective of the dynamic behavior of SULT2A1 structures. Structural stability and network analyses indicated that the cooperation between PAP and LCA may enhance the thermal stability and compact communication in enzymes. Molecular dynamic simulations, docking study using the crystal structure of the SULT2A1 complex with PAP and lithocholic acid (LCA) (PDB ID 3F3Y). The free SULT2A1 and binary complexes (SULT2A1/LCA and SULT2A1/PAP) are derived from the crystal structure of the SULT2A1 complex with both PAP and LCA (PDB ID3F3Y), modeling, detailed overview. The smaller substrates such as LCA could bind stably to the active pocket in the presence of PAP. The substrates or inhibitors with a large spatial structure need to bind to the open conformation (without PAP) prior to PAPS binding | Homo sapiens |
2.8.2.2 | physiological function | cytosolic sulfotransferases (SULTs) act as phase II metabolic enzymes | Homo sapiens |