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Normand, T ; Husen, B ; Leenders, F ; Pelczar, H ; Baert, JL ; Begue, A ; Flourens, AC ; Adamski, J ; deLaunoit, Y

Molecular characterization of mouse 17 beta-hydroxysteroid dehydrogenase IV

Journal of Steroid Biochemistry and Molecular Biology 55 (5-6) 541-548

par Administrateur - publié le

Abstract :

17 beta-hydroxysteroid dehydrogenases (17 beta-HSD) catalyze the conversion of estrogens and androgens at the C17 position. The 17 beta-HSD type I, II, III and IV share less than 25% amino acid similarity. The human and porcine 17 beta-HSD N reveal a three-domain structure unknown among other dehydrogenases. The N-terminal domains resemble the short chain alcohol dehydrogenase family while the central parts are related to the C-terminal parts of enzymes involved in peroxisomal beta-oxidation of fatty acids and the C-terminal domains are similar to sterol carrier protein 2. We describe the cloning of the mouse 17 beta-HSD IV cDNA and the expression of its mRNA.