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Estrone sulfotransferase

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Estrone sulfotransferase
Identifiers
EC no.2.8.2.4
CAS no.9026-06-6
Alt. namesEstrogen sulfotransferase; EST
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

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

Reaction

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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

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

Function

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Distribution of STSTooltip steroid sulfatase and EST activities for interconversion of estradiol and estrone in adult human tissues.[3]

Structure

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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

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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

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References

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  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. 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
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  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

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