{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSULT2A1 is a key cytosolic sulfotransferase that catalyzes the sulfonation of endogenous hydroxysteroids—most notably converting dehydroepiandrosterone (DHEA) into its circulating sulfate (DHEA‐S)—as well as bile acids and various xenobiotics. Detailed kinetic studies in stable cell systems have demonstrated its Michaelis–Menten behavior with marked variations in substrate affinity, and its reactions extend to both classical O‐sulfation as well as N‐sulfation of amine‐containing drugs. In addition, SULT2A1 is capable of sulfating non‐canonical substrates such as 4‐ketosteroids via keto–enol isomerization, and its activity is subject to inhibition by antiandrogen compounds. Furthermore, efficient DHEA sulfation has been shown to depend on enzyme–cofactor coupling with PAPSS2, emphasizing the physiological relevance of both substrate orientation and cofactor availability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural and mechanistic investigations have revealed that SULT2A1’s catalytic efficiency is tightly linked to the conformational dynamics of its active-site “cap” and the precise orientation of substrates within its dual binding pockets. Mutagenesis studies—targeting critical residues involved in substrate–enzyme interactions—have uncovered alternate binding modes that underlie substrate inhibition, while molecular dynamics and redox analyses have demonstrated that disulfide bond formation and active-site isomerization modulate both ligand binding and thermal stability. Complementary density functional theory calculations further underscore the importance of hydrogen bond interactions in stabilizing substrate conformations within the active site."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRegulation of SULT2A1 occurs in a tissue- and context-dependent manner, primarily via transcriptional control by multiple nuclear receptors and transcription factors. Investigations have identified positive regulatory effects by factors such as thyroid hormone (via SF1), retinoid-related orphan receptors, and liver X receptor α, whereas other studies demonstrate that ERRα may repress promoter activity. Moreover, genetic polymorphisms in SULT2A1 are linked to inter-individual differences in circulating DHEA-S levels and have been associated with conditions including polycystic ovary syndrome, altered neurosteroid profiles in attention-deficit/hyperactivity disorder, and hepatocellular carcinoma, where SULT2A1 deficiency appears to promote tumor stemness and chemoresistance. In addition, in situ analyses of adrenal tissues further emphasize the clinical significance of SULT2A1 expression patterns in steroidogenic regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Peter H Rehse, Ming Zhou, Sheng-Xiang Lin "}, {"type": "b", "children": [{"type": "t", "text": "Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/bj3640165"}], "href": "https://doi.org/10.1042/bj3640165"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11988089"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11988089"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Karla J Saner, Takashi Suzuki, Hironobu Sasano, et al. 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