Abstract
Oestradiol-17β hydroxysteroid dehydrogenase (EC 1.1.1.62) is involved in the glandular synthesis of oestradiol. Oestradiol dehydrogenase also has a pivotal role in regulating tissue concentrations of this biologically active oestrogen, mediating the conversion of oestrone to oestradiol or metabolism of oestradiol to oestrone. In addition to the ovary and testis, oestradiol dehydrogenase activity is detectable in many human tissues including the placenta, endometrium, lung, prostate and breast. Recent advances in molecular endocrinology have provided some intriguing insights into the possible ancestry of this enzyme but important questions about the control of its activity still remain unanswered. The steroid dehydrogenase family Two human placental oestradiol dehydrogenase cDNA clones have now been isolated and a unique primary structure of 327 amino acids has been deduced from the nucleotide sequence (Peltoketo, Isomaa, Mäenausta & Vihko, 1988; Luu-The, Labrie, Zhao et al. 1989). Based upon measurements of enzyme activity, multiple forms of oestradiol dehydrogenase have

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