{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kurogi K"],"funding":["JSPS KAKENHI"],"pagination":["pgae097"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10939482"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(3)"],"pubmed_abstract":["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 <i>O</i>-sulfonation of hydroxy groups or <i>N</i>-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of <i>C</i>-sulfonation of α,β-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 α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the <i>C</i>-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<sub>2</sub> exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of <i>C</i>-sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs."],"journal":["PNAS nexus"],"pubmed_title":["A new type of sulfation reaction: <i>C</i>-sulfonation for α,β-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1."],"pmcid":["PMC10939482"],"funding_grant_id":["15H04502","21H02119 for","17H05028","25850074","21580114","23580138"],"pubmed_authors":["Kanekiyo M","Kurogi K","Fukusaki E","Kakuta Y","Sakakibara Y","Matsumoto J","Hashiguchi T","Bamba T","Suiko M","Teramoto T","Fukushima T","Kataoka H"],"additional_accession":[]},"is_claimable":false,"name":"A new type of sulfation reaction: <i>C</i>-sulfonation for α,β-unsaturated carbonyl groups by a novel sulfotransferase SULT7A1.","description":"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 <i>O</i>-sulfonation of hydroxy groups or <i>N</i>-sulfonation of amino groups of substrate compounds. In this study, we report the discovery of <i>C</i>-sulfonation of α,β-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 α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the <i>C</i>-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<sub>2</sub> exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of <i>C</i>-sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-02T07:02:05.591Z","creation":"2026-04-15T03:15:35.857Z"},"accession":"S-EPMC10939482","cross_references":{"pubmed":["38487162"],"doi":["10.1093/pnasnexus/pgae097"]}}