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Many enzymes catalyse reactions that have an oestrogen as a substrate and/or a product. The reactions catalysed include aromatisation, oxidation, reduction, sulfonation, desulfonation, hydroxylation and methoxylation. The enzymes that catalyse these reactions must all recognise and bind oestrogen but, despite this, they have diverse structures. This review looks at each of these enzymes in turn, describing the structure and discussing the mechanism of the catalysed reaction. Since oestrogen has a role in many disease states inhibition of the enzymes of oestrogen metabolism may have an impact on the state or progression of the disease and inhibitors of these enzymes are briefly discussed. This article is part of a Special Issue entitled 'CSR 2013'.

Original publication




Journal article


J Steroid Biochem Mol Biol

Publication Date





27 - 49


17β-HSD, 17β-Hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase, 3,5-dinitrocatechol, 3-(((8R,9S,13S,14S,16R,17S)-3,17-dihydroxy-13-methyl-7,8,9,11,12,13,14,15,16,17-decahydro-6H-cyclopenta[a]phenanthren-16-yl)methyl)benzamide, 3′-phosphoadenosine-5′-phosphate, 3′-phosphoadenosine-5′-phosphosulfate, Aromatase, COMT, DHEA(S), DHETNA, DNC, E1(S), E2(S), E2B, E3, E4, ER, FAD/FMN, FG, HFG(S), NADP(+), NADPH, O5′-[9-(3,17β-dihydroxy-1,3,5(10)-estratrien-16β-yl)-nonanoyl]adenosine, Oestrogen, PAP, PAPS, Protein structure, Reaction mechanism, S-adenosyl methionine, SAM, SDR, Sulfatase, Sulfotransferase, catechol-O-methyl transferase, dehydroepiandrosterone (sulfate), estetrol, estradiol (sulfate), estriol, estrogen receptor, estrone (sulfate), flavin adenine dinucleotide/flavin mononucleotide, formylglycine, hydroxyformylglycine (sulfate), mb-COMT, membrane-bound COMT, nicotinamide adenine dinucleotide phosphate (oxidised), nicotinamide adenine dinucleotide phosphate (reduced), s-COMT, short-chain dehydrogenase/reductase, soluble COMT, 17-Hydroxysteroid Dehydrogenases, Amino Acid Sequence, Animals, Aromatase, Biocatalysis, Catechol O-Methyltransferase, Estrogens, Humans, Hydroxylation, Models, Molecular, Molecular Sequence Data, Molecular Structure, Sequence Homology, Amino Acid, Steryl-Sulfatase, Sulfotransferases