IPR011348
17beta-dehydrogenase
InterPro entry
Short name | 17beta_DH |
Overlapping homologous superfamilies | |
family relationships |
Description
This entry represents 17beta-hydroxysteroid dehydrogenases (17B-HSDs), a group of enzymes which catalyse the last step in the biosynthesis of all androgens and estrogens -the reversible NAD(P)-linked transfer of a hydride to and from the 17-position of steroid molecules
[1]. A total of six isozymes have been identified which vary in substrate specificity, tissue specificity and preferred direction of the reaction.
The most intensively studied enzyme in this entry is human estrogenic 17beta-hydroxysteroid dehydrogenase (
P14061) which is responsible for the last step in the synthesis of all estrogens. As active estrogens stimulate the proliferation of breast cancer cells, this enzyme is a potential target for drugs to treat breast cancer
[2]. It is a membrane-associated homodimer which posseses the Tyr-X-X-X-Lys motif typical of short-chain dehydrogenases and forms a typical Rossman fold
[3].
This family also includes Retinol dehydrogenase 8 which is closely related to 17-beta-hydroxysteroid dehydrogenase 1
[4].
References
1.Expression and regulation of 17 beta-hydroxysteroid dehydrogenase type 1. Peltoketo H, Isomaa V, Poutanen M, Vihko R. J. Endocrinol. 150 Suppl, S21-30, (1996). PMID: 8943783
2.Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+. Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D. Proc. Natl. Acad. Sci. U.S.A. 96, 840-5, (1999). View articlePMID: 9927655
3.Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX. Structure 3, 503-13, (1995). View articlePMID: 7663947
GO terms
biological process
molecular function
cellular component
Cross References
Contributing Member Database Entry
- PIRSF:PIRSF000095