Estrone sulfotransferase
Estrone sulfotransferase (EST) (EC 2.8.2.4), also known as estrogen sulfotransferase, is an enzyme that catalyzes the transformation of an unconjugated estrogen like estrone into a sulfated estrogen like estrone sulfate. It is a steroid sulfotransferase and belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. This enzyme participates in androgen and estrogen metabolism and sulfur metabolism.
| Estrone sulfotransferase | |
|---|---|
| Identifiers | |
| EC no. | 2.8.2.4 |
| CAS no. | 9026-06-6 |
| Alt. names | Estrogen sulfotransferase; EST |
| Databases | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PRIAM | profile |
| PDB structures | RCSB PDB PDBe PDBsum |
| Gene Ontology | AmiGO / QuickGO |
Steroid sulfatase is an enzyme that catalyzes the reverse reaction, the transfer of a sulfate to an unconjugated estrogen.
Reaction edit
In enzymology, an EST is an enzyme that catalyzes the following chemical reaction:
- 3'-phosphoadenylyl sulfate + estrone adenosine 3',5'-bisphosphate + estrone 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and estrone, whereas its two products are adenosine 3',5'-bisphosphate and estrone 3-sulfate.
The enzyme also catalyzes the same reaction for estradiol, with estradiol sulfate as the product.
Types edit
Two enzymes have been identified that together are thought to represent estrone sulfotransferase (EST):[1][2]
- SULT1A1 (catalyzes the reactions estradiol to estradiol sulfate and, to a lesser extent than SULT1E1, estrone to estrone sulfate)
- SULT1E1 (catalyzes the reactions estrone to estrone sulfate and estradiol to estradiol sulfate)
Function edit
Structure edit
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1AQU, 1AQY, 1BO6, 1G3M, and 1HY3.
Names edit
The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:estrone 3-sulfotransferase. Other names in common use include 3'-phosphoadenylyl sulfate-estrone 3-sulfotransferase, estrogen sulfotransferase, estrogen sulphotransferase, oestrogen sulphotransferase, and 3'-phosphoadenylylsulfate:oestrone sulfotransferase.
See also edit
References edit
- ^ Mueller JW, Gilligan LC, Idkowiak J, Arlt W, Foster PA (2015). "The Regulation of Steroid Action by Sulfation and Desulfation". Endocr. Rev. 36 (5): 526–63. doi:10.1210/er.2015-1036. PMC 4591525. PMID 26213785.
- ^ EC 2.8.2.4 – estrone sulfotransferase and Organism(s) Homo sapiens. Technische Universität Braunschweig. January 2018. Retrieved 10 August 2018.
Substrate: 3'-phosphoadenylyl sulfate + estrone
Product: adenosine 3',5'-bisphosphate + estrone 3-sulfate
Organism: Homo sapiens
Commentary (substrate): high activity by SULT1E1, low activity by phenol sulfotransferase SULT1A1, EC 2.8.2.1{{cite encyclopedia}}:|website=ignored (help) - ^ Miki Y, Nakata T, Suzuki T, Darnel AD, Moriya T, Kaneko C, Hidaka K, Shiotsu Y, Kusaka H, Sasano H (December 2002). "Systemic distribution of steroid sulfatase and estrogen sulfotransferase in human adult and fetal tissues". J. Clin. Endocrinol. Metab. 87 (12): 5760–8. doi:10.1210/jc.2002-020670. PMID 12466383.
Further reading edit
- Adams JB, Poulos A (1967). "Enzymic synthesis of steroid sulphates. 3. Isolation and properties of estrogen sulphotransferase of bovine adrenal glands". Biochim. Biophys. Acta. 146 (2): 493–508. doi:10.1016/0005-2744(67)90233-1. PMID 4965224.
- Rozhin J, Zemlicka J, Brooks SC (1967). "Studies on bovine adrenal estrogen sulfotransferase. Inhibition and possible involvement of adenine-estrogen stacking". J. Biol. Chem. 252 (20): 7214–7220. doi:10.1016/S0021-9258(19)66957-7. PMID 903358.
- Adams JB, Ellyard RK, Low J (1974). "Enzymic synthesis of steroid sulphates. IX. Physical and chemical properties of purified oestrogen sulphotransferase from bovine adrenal glands, the nature of its isoenzymic forms and a proposed model to explain its wave-like kinetics". Biochim. Biophys. Acta. 370 (1): 160–88. doi:10.1016/0005-2744(74)90042-4. PMID 4473218.