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- W91716571 abstract "Publisher Summary This chapter describes the nature and function of human placental 17β-estradiol dehydrogenase enzyme. It has been found that human term placenta is very rich in an enzyme that oxidizes estradiol to estrone. Moreover, a 50-fold purification of this enzyme is named 17β-estradiol dehydrogenase. It catalyzes the reversible interconversion of 17β-estradiol and estrone and utilizes either diphosphopyridine nucleotide or triphosphopyridine nucleotide as cofactor. Although the physiological functions of this enzyme are unknown, it is evident that any enzyme that can interconvert biologically active and relatively inactive molecules is a potential candidate for an important physiological regulatory role. Its action or lack of action upon steroids chemically related to estradiol may reflect possible functions in the biogenesis or degradation of steroidal estrogens in the human placenta. Most studies dealing with the substrate binding sites of enzymes have been carried out with enzymes that catalyze reactions involving either small charged molecules or charged macromolecules." @default.
- W91716571 created "2016-06-24" @default.
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- W91716571 date "1974-01-01" @default.
- W91716571 modified "2023-10-18" @default.
- W91716571 title "Human Placental 17β-Estradiol Dehydrogenase: Characterization and Structural Studies" @default.
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- W91716571 doi "https://doi.org/10.1016/b978-0-12-571130-2.50008-0" @default.
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