Molecular cloning of a novel widely expressed human 80 kDa 17 β -hydroxysteroid dehydrogenase IV

Abstract : Reactions of oestrogens and androgens at position C-17 are catalysed by 17 beta-hydroxysteroid dehydrogenases (17 beta-HSDs). Cloning of the cDNA of a novel human 17 beta-HSD IV and expression of its mRNA are described. A probe derived from the recently discovered porcine 17 beta-oestradiol dehydrogenase (17 beta-EDH) was used to isolate a 2.6 kb human cDNA encoding a continuous protein of 736 amino acids of high (84%) similarity to the porcine 17 beta-EDH. The calculated molecular mass of the human enzyme is 79,595 Da. Other sequence similarities shared by the two enzymes are: an N-terminal sequence which is similar to that of members of the short-chain alcohol dehydrogenase family; amino acids 343-607 which are similar to the C-terminal domains of a trifunctional Candida tropicalis enzyme and the FOX2 gene product of Saccharomyces cerevisiae; amino acids 596-736 which are similar to human sterol carrier protein 2. The previously cloned human 17 beta-HSD I, II and III are less than 25% identical with 17 beta-HSD IV. mRNA for HSD IV is a single species of 3.0 kb, present in many tissues with highest concentrations in liver, heart, prostate and testes. When over-expressed in mammalian cells, the human 17 beta-HSD IV enzyme displays a specific unidirectional oxidative 17 beta-HSD activity.
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https://hal.archives-ouvertes.fr/hal-02160026
Contributor : Laëtitia Legoupil <>
Submitted on : Wednesday, June 19, 2019 - 11:50:47 AM
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J Adamski, Thierry Normand, F Leenders, D Monté, A. Bégué, et al.. Molecular cloning of a novel widely expressed human 80 kDa 17 β -hydroxysteroid dehydrogenase IV. Biochemical Journal, Portland Press, 1995, 311 (2), pp.437-443. ⟨10.1042/bj3110437⟩. ⟨hal-02160026⟩

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