InterPro : IPR011348

Name  17beta-dehydrogenase Short Name  17beta_DH
Type  Family 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 []. 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 () 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 []. 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 [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR020904 Short-chain dehydrogenase/reductase, conserved site Sc_DH/Rdtase_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002347 Glucose/ribitol dehydrogenase Glc/ribitol_DH Family

3 Publications

First Author Title Year Journal Volume Pages
Ghosh D Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. 1995 Structure 3 503-13
Sawicki MW 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+. 1999 Proc Natl Acad Sci U S A 96 840-5
Peltoketo H Expression and regulation of 17 beta-hydroxysteroid dehydrogenase type 1. 1996 J Endocrinol 150 Suppl S21-30



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)