Analysis and characteristics of multiple types of human 17beta-hydroxysteroid dehydrogenase.

Abstract

Androgens and estrogens are not only synthesized in the gonads but also in peripheral target tissues. Accordingly, recent molecular cloning has allowed us to identify multiple types of 17beta-hydroxysteroid dehydrogenases (17beta-HSD), the key and exclusive enzymes involved in the formation and inactivation of sex steroids. However, only one form, namely, type 3 17beta-HSD, is responsible for pseudohermaphroditism in deficient boys. To date, seven human 17beta-HSDs have been isolated and characterized. Although they catalyze substrates having a similar structure, 17beta-HSDs have very low homology. In intact cells in culture, these enzymes catalyze the reaction in a unidirectional way - types 1, 3, 5 and 7 catalyze the reductive reaction, while types 2, 4 and 8 catalyze the oxidative reaction. It is noteworthy that rat type 6 17beta-HSD also catalyzes the reaction in the oxidative direction. In this report, we analyze the different characteristics of the multiple types of human 17beta-HSD.

• Authors: V Luu-The
• Journal: The Journal of steroid biochemistry and molecular biology (J Steroid Biochem Mol Biol) 2001 Jan-Mar Vol. 76 Issue 1-5 Pg. 143-51 ISSN: 0960-0760 [Print] England
• PMID: 11384872 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Androgens
• Estrogens
• Isoenzymes
• 17-Hydroxysteroid Dehydrogenases
• 3 (or 17)-beta-hydroxysteroid dehydrogenase

Topics

• 17-Hydroxysteroid Dehydrogenases (metabolism)
• Androgens (biosynthesis)
• Estrogens (biosynthesis)
• Humans
• Isoenzymes (metabolism)