| EC |
1.1.1.62 |
| Accepted name: |
17β-estradiol 17-dehydrogenase |
| Reaction: |
17β-estradiol + NAD(P)+ = estrone + NAD(P)H + H+ |
| Other name(s): |
20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7 |
| Systematic name: |
17β-estradiol:NAD(P)+ 17-oxidoreductase |
| Comments: |
The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase [3]. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+. |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-61-9 |
| References: |
| 1. |
Kautsky, M.P. and Hagerman, D.D. 17β-Estradiol dehydrogenase of ovine ovaries. J. Biol. Chem. 245 (1970) 1978–1984. [PMID: 4314937] |
| 2. |
Langer, L.J., Alexander, J.A. and Engel, L.L. Human placental estradiol-17β dehydrogenase. II. Kinetics and substrate specificities. J. Biol. Chem. 234 (1959) 2609–2614. [PMID: 14413943] |
| 3. |
Marijanovic, Z., Laubner, D., Moller, G., Gege, C., Husen, B., Adamski, J. and Breitling, R. Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol. Endocrinol. 17 (2003) 1715–1725. [DOI] [PMID: 12829805] |
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| [EC 1.1.1.62 created 1965, modified 1983, modified 1986, modified 2012] |
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