5x2b: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/B7ZWN4_MOUSE B7ZWN4_MOUSE] | [https://www.uniprot.org/uniprot/B7ZWN4_MOUSE B7ZWN4_MOUSE] | ||
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== Publication Abstract from PubMed == | |||
Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the O-sulfonation of hydroxy groups or N-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of C-sulfonation of alpha,beta-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3'-phosphoadenosine 5'-phosphosulfate to the alpha-carbon of alpha,beta-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the C-sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J(2) exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of alpha,beta-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of C-sulfonation of alpha,beta-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs. | |||
A new type of sulfation reaction: C-sulfonation for alpha,beta-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1.,Kurogi K, Sakakibara Y, Hashiguchi T, Kakuta Y, Kanekiyo M, Teramoto T, Fukushima T, Bamba T, Matsumoto J, Fukusaki E, Kataoka H, Suiko M PNAS Nexus. 2024 Mar 4;3(3):pgae097. doi: 10.1093/pnasnexus/pgae097. eCollection , 2024 Mar. PMID:38487162<ref>PMID:38487162</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | *[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | ||
== References == | |||
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</StructureSection> | </StructureSection> | ||
