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  • Title: Aromatization of delta4-androstene-3,17-dione, 19-hydroxy-delta4-androstene-3,17-dione, and 19-oxo-delta4-androstene-3,17-dione at a common catalytic site in human placental microsomes.
    Author: Kelly WG, Judd D, Stolee A.
    Journal: Biochemistry; 1977 Jan 11; 16(1):140-5. PubMed ID: 831774.
    Abstract:
    Estrogen is believed to be biosynthesized from androstenedione in placental microsomes by a multienzyme pathway in which 19-hydroxyandrostenedione and 19-oxoandrostenedione (or the hydrated form) are obligatory intermediates. However, both 19-hydroxyandrostenedione and 19-oxoandrostenedione competitively inhibited aromatization of androstenedione, and all three steroids were shown to be mutually competitive. 19-Hydroxyandrostenedione and 19-oxoandrostenedione also competed with androstenedione for binding sites in the microsomes at 4 degrees C. In confirmation of the work of Hollander (Hollander, N. (1962), Endocrinology 71, 723-728), and of Osawa and Shibata (Osawa, Y., and Shibata, K., (1973), Abstracts of the 55th Meeting of the Endocrine Society, Abstract 116) when androstenedione and 19-hydroxyandrostenedione were incubated together, both were converted to estrogen, but little androstenedione was converted to 19-hydroxyandrostenedione. Considered together, these results are incompatible with the multienzyme pathway. Rather, these results may be explained by aromatization of androstenedione at a single catalytic site via enzyme-bound transition states. Both proposed intermediates are, according to this view, by-products which can also be aromatized.
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