Estrone sulfotransferase explained

Estrone sulfotransferase
Altnames:	Estrogen sulfotransferase; EST
Ec Number:	2.8.2.4
Cas Number:	9026-06-6
Go Code:	0004304

Estrone sulfotransferase (EST), 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

In enzymology, an EST is an enzyme that catalyzes the following chemical reaction:

3'-phosphoadenylyl sulfate + estrone

\rightleftharpoons 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]}

• 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

Structure

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes,,,, and .

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.

See also

• Steroidogenic enzyme

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 . 493 - 508 . 4965224 . 2 . 10.1016/0005-2744(67)90233-1 .
• 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 . 10.1016/S0021-9258(19)66957-7 . 903358 . free .
• 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 . 160 - 88 . 4473218 . 1 . 10.1016/0005-2744(74)90042-4 .

Notes and References

1. Mueller JW, Gilligan LC, Idkowiak J, Arlt W, Foster PA . The Regulation of Steroid Action by Sulfation and Desulfation . Endocr. Rev. . 36 . 5 . 526–63 . 2015 . 26213785 . 4591525 . 10.1210/er.2015-1036 .
2. Encyclopedia: EC 2.8.2.4 – estrone sulfotransferase and Organism(s) Homo sapiens. BRENDA. Technische Universität Braunschweig. 10 August 2018. January 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.