EC 1.1.1.62 - 17β-estradiol 17-dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.62

Names

Accepted name:
17β-estradiol 17-dehydrogenase
Other names:
17β,20α-hydroxysteroid dehydrogenase
17β-HSD
17β-estradiol dehydrogenase
20α-hydroxysteroid dehydrogenase
estradiol dehydrogenase
estrogen 17-oxidoreductase
17β-hydroxysteroid dehydrogenase
HSD17B7
Systematic name:
17β-estradiol:NAD(P)+ 17-oxidoreductase

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004303
CAS Registry Number: 9028-61-9
UniProtKB/Swiss-Prot: (37) [show] [UniProt]

References

  1. Kautsky, M.P. and Hagerman, D.D.
    17β-Estradiol dehydrogenase of ovine ovaries.
    J. Biol. Chem. 245: 1978-1984 (1970). [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: 2609-2614 (1959). [PMID: 14413943]
  3. Marijanovic, Z., Laubner, D., Moller, G., Gege, C., Husen, B., Adamski, J., Breitling, R.
    Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis.
    Mol. Endocrinol. 17: 1715-1725 (2003). [PMID: 12829805]

[EC 1.1.1.62 created 1965, modified 1983, modified 1986, modified 2012]