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 number2.8.2.4
CAS number9026-06-6
Alt. namesEstrogen sulfotransferase; EST
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Steroid sulfatase is an enzyme that catalyzes the reverse reaction, the transfer of a sulfate to an unconjugated estrogen.

Reaction

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

Two enzymes have been identified that together are thought to represent estrone sulfotransferase (EST):[1][2]

Function
Distribution of STS and EST activities for interconversion of estradiol and estrone in adult human tissues.[3]

Structure

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

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.

gollark: However, do NOT give people printers or devices related to printers.
gollark: Hmm, that's actually quite artistic, good job.
gollark: Yes, trivially, via encoding of bytes into unary.
gollark: Yes, you said.
gollark: I could buy very moderately good GPUs for that much money.

See also

References
  1. 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.
  2. "EC 2.8.2.4 – estrone sulfotransferase and Organism(s) Homo sapiens". BRENDA. 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
  3. 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
  • 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: 7214–7220.
  • 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.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.