Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme.

Abstract

Very recently, the mouse 17alpha-hydroxysteroid dehydrogenase (m17alpha-HSD), a member of the aldo-keto reductase (AKR) superfamily, has been characterized and identified as the unique enzyme able to catalyze efficiently and in a stereospecific manner the conversion of androstenedione (Delta4) into epitestosterone (epi-T), the 17alpha-epimer of testosterone… (More)

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@article{Faucher2006CrystalSO, title={Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme.}, author={Fr{\'e}d{\'e}rick Faucher and Karine Pereira de J{\'e}sus-Tran and Line Cantin and Van Luu-The and Fernand Labrie and Rock Breton}, journal={Journal of molecular biology}, year={2006}, volume={364 4}, pages={747-63} }