Steroid sulfotransferase

In enzymology, a steroid sulfotransferase (EC 2.8.2.15) is an enzyme that catalyzes the chemical reaction

steroid sulfotransferase
Identifiers
EC no.2.8.2.15
CAS no.9032-76-2
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IntEnzIntEnz view
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MetaCycmetabolic pathway
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3'-phosphoadenylyl sulfate + a phenolic steroid adenosine 3',5'-bisphosphate + steroid O-sulfate

Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenolic steroid, whereas its two products are adenosine 3',5'-bisphosphate and steroid O-sulfate.

This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase. This enzyme is also called steroid alcohol sulfotransferase. This enzyme participates in steroid metabolism.

Genes

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Of 62 sulfotransferase genes in the human genome, 16 represent cytoplasmic sulfotransferases, and of these 16 cytoplasmic sulfotransferases, five have been found to act as steroid sulfotransferases.[1] These five sulfotransferase genes are SULT1A1, SULT1E1, and SULT2A1, as well as the two isoforms of SULT2B1, SULT2B1a and SULT2B1b.[1] Their substrate specificity is as follows:[1]

Traditionally, steroid sulfotransferases have been named according to their preferred substrate, for instance estrogen sulfotransferase (SULT1E1) and DHEA sulfotransferase (SULT2A1).[1] However, cytosolic steroid sulfotransferases show broad substrate specificity, and SULT1E1 and SULT2A1 are not the only steroid sulfotransferases that sulfate estrogens and DHEA, respectively.[1]

See also

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References

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  1. ^ a b c d e 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.
  • Adams JB, McDonald D (1980). "Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals". Biochim. Biophys. Acta. 615 (1): 275–8. doi:10.1016/0005-2744(80)90031-5. PMID 6932974.