| UniProt functional annotation for P49888 | |||
| UniProt code: P49888. |
| Organism: | Homo sapiens (Human). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. | |
| Function: | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone (PubMed:7779757, PubMed:11884392, PubMed:11006110). Is a key enzyme in estrogen homeostasis, the sulfation of estrogens leads to their inactivation. Also sulfates dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol and xenobiotic compounds like ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at significantly lower efficiency (PubMed:11006110, PubMed:19589875). Does not sulfonate cortisol, testosterone and dopamine (PubMed:7779757, PubMed:11006110). {ECO:0000269|PubMed:11006110, ECO:0000269|PubMed:11884392, ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:7779757}. | |
| Catalytic activity: | Reaction=3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'- bisphosphate + estrone 3-sulfate + H(+); Xref=Rhea:RHEA:15973, ChEBI:CHEBI:15378, ChEBI:CHEBI:17263, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:60050; EC=2.8.2.4; Evidence={ECO:0000269|PubMed:11006110, ECO:0000269|PubMed:11884392, ECO:0000269|PubMed:7779757}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974; Evidence={ECO:0000305|PubMed:11884392}; | |
| Catalytic activity: | Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)- hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567; Evidence={ECO:0000269|PubMed:19589875}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349; Evidence={ECO:0000305|PubMed:19589875}; | |
| Catalytic activity: | Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta- estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582; Evidence={ECO:0000269|PubMed:11006110, ECO:0000269|PubMed:7779757}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373; Evidence={ECO:0000305|PubMed:7779757}; | |
| Catalytic activity: | Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one = 3beta-sulfooxy-androst-5-en-17-one + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:11006110}; | |
| Activity regulation: | Inhibited by estradiol. {ECO:0000269|PubMed:11006110}. | |
| Biophysicochemical properties: | Kinetic parameters: KM=0.3 uM for 17beta-estradiol {ECO:0000269|PubMed:11006110}; KM=0.2 uM for estrone {ECO:0000269|PubMed:11006110}; KM=0.2 uM for DHEA {ECO:0000269|PubMed:11006110}; KM=32220 uM for dopamine {ECO:0000269|PubMed:11006110}; KM=76.6 uM for p-nitrophenol {ECO:0000269|PubMed:11006110}; KM=0.9 uM for (24S)-hydroxycholesterol {ECO:0000269|PubMed:19589875}; KM=0.66 uM for PAPS {ECO:0000269|PubMed:11884392}; KM=0.46 uM for PAPS {ECO:0000269|PubMed:11006110}; Vmax=37.2 nmol/min/mg enzyme with 17beta-estradiol {ECO:0000269|PubMed:11006110}; Vmax=16.3 nmol/min/mg enzyme with estrone {ECO:0000269|PubMed:11006110}; Vmax=5.5 nmol/min/mg enzyme with DHEA {ECO:0000269|PubMed:11006110}; Vmax=13.3 nmol/min/mg enzyme with dopaminne; Vmax=135.9 nmol/min/mg enzyme with p-nitrophenol {ECO:0000269|PubMed:11006110}; Note=Kcat is 55 min(-1) with (24S)-hydroxycholesterol. {ECO:0000269|PubMed:19589875}; | |
| Subunit: | Homodimer. {ECO:0000269|PubMed:11884392, ECO:0000269|PubMed:12782487}. | |
| Subcellular location: | Cytoplasm, cytosol {ECO:0000269|PubMed:11006110}. | |
| Tissue specificity: | Liver, intestine and at lower level in the kidney. | |
| Similarity: | Belongs to the sulfotransferase 1 family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.