Structural basis for androgen specificity and oestrogen synthesis in human aromatase

Debashis Ghosh (), Jennifer Griswold, Mary Erman and Walter Pangborn
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Debashis Ghosh: Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA
Jennifer Griswold: Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA
Mary Erman: Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA
Walter Pangborn: Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA

Nature, 2009, vol. 457, issue 7226, 219-223

Abstract: Human placental aromatase structure Aromatase cytochrome P450 is the only enzyme in vertebrates known to catalyse the biosynthesis of all oestrogens from androgens. This enzyme catalyses the three-step conversion of androstenedione, testosterone, and 16α-hydroxytestosterone to oestrone, 17β-oestradiol, and 17β,16α-oestriol (respectively). Inhibitors of aromatase are potential therapeutics for oestrogen-dependent breast cancer. In this paper, Ghosh et al. solve the X-ray crystal structure of the first natural mammalian, full-length P450, human placental aromatase. The locations of catalytically important residues shed new light on the reaction mechanism of this enzyme, and it may be possible to utilize this information to develop new aromatase inhibitors.

Date: 2009
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DOI: 10.1038/nature07614

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