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1.1.1.62: 17beta-estradiol 17-dehydrogenase

This is an abbreviated version!
For detailed information about 17beta-estradiol 17-dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.62

Reaction

17beta-estradiol
+
NAD(P)+
=
estrone
 +
NAD(P)H
 +
H+

Synonyms

(17beta-HSD) type 1, (17beta-HSD) type 2, 17-beta-HSD 2, 17-beta-hydroxysteroid dehydrogenase type 12, 17-beta-hydroxysteroid dehydrogenase type 2, 17-HOR, 17-HSD, 17beta HSD1, 17beta,20alpha-hydroxysteroid dehydrogenase, 17beta-estradiol dehydrogenase, 17beta-HSD, 17beta-hsd 14, 17beta-HSD I, 17beta-HSD type 1, 17beta-HSD type 12, 17beta-HSD type 2, 17beta-HSD type 4, 17beta-HSD type 5, 17beta-HSD type 7, 17beta-HSD type 8, 17beta-HSD1, 17beta-HSD10, 17beta-HSD12, 17beta-HSD14, 17beta-HSD2, 17beta-HSD4, 17beta-HSD5, 17beta-HSD7, 17beta-HSD7 2, 17beta-HSDcl, 17beta-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase 1, 17beta-hydroxysteroid dehydrogenase 2, 17beta-hydroxysteroid dehydrogenase 4, 17beta-hydroxysteroid dehydrogenase type 1, 17beta-hydroxysteroid dehydrogenase type 10, 17beta-hydroxysteroid dehydrogenase type 12, 17beta-hydroxysteroid dehydrogenase type 14, 17beta-hydroxysteroid dehydrogenase type 2, 17beta-hydroxysteroid dehydrogenase type 4, 17beta-hydroxysteroid dehydrogenase type 5, 17beta-hydroxysteroid dehydrogenase type 6, 17beta-hydroxysteroid dehydrogenase type 7, 17beta-hydroxysteroid dehydrogenase type 8, 17beta-hydroxysteroid dehydrogenase type I, 17beta-hydroxysteroid dehydrogenase type IV, 17beta-hydroxysteroid dehydrogenase types 1, 17beta-hydroxysteroid dehydrogenases type 1, 17betaHSD, 17betaHSD1, 17betaHSD14, 17betaHSD6, 17HSD1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, 20alpha-hydroxysteroid dehydrogenase, 3beta-HSD, 3beta-hydroxysteroid dehydrogenase, 3betaHSD, 7beta-HSD type 1, 7beta-HSD7, AKR1B15, AKR1C1, AKR1C2, AKR1C3, AKR1C4, aldo-keto reductase 1B15, C6Y55_RS00895, C6Y55_RS01070, C6Y55_RS01190, C6Y55_RS15130, dehydrogenase, estradiol 17beta-, E2DH, EDH, estradiol 17beta-dehydrogenase, estradiol dehydrogenase, estrogen 17-oxidoreductase, estrogenic 17beta-hydroxysteroid dehydrogenase, form 2 type 7 17beta-hydroxysteroid dehydrogenase, HSD17B1, HSD17B12, HSD17B2, HSD17B4, HSD17B7, hydroxysteroid (17-beta) dehydrogenase 1, Ke6 protein, mf17beta-HSD12, microsomal 17-beta-hydroxysteroid dehydrogenase, More, NlHsd17b12, oestradiol-17beta hydroxysteroid dehydrogenase, placental 17-beta-hydroxysteroid dehydrogenase, PRAP, PRL receptor associated protein, reductive 17beta-hydroxysteroid dehydrogenase type 7, testicular 17-beta-hydroxysteroid dehydrogenase, type 1 17beta-HSD, type 1 17beta-hydroxysteroid dehydrogenase, type 12 17beta-HSD, type 12 17beta-hydroxysteroid dehydrogenase, type 2 3alpha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 5 17-hydroxysteroid dehydrogenase/prostaglandin F synthase, type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase, type 7 17beta-hydroxysteroid dehydrogenase, type 8 17beta-HSD, type 8 17beta-hydroxysteroid dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.62 17beta-estradiol 17-dehydrogenase

Crystallization

Crystallization on EC 1.1.1.62 - 17beta-estradiol 17-dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, crystallization of the 17beta-HSDcl apo form and Tyr167Phe mutant, crystals diffract to 1.7 A resolution. The space group is identified as I4(1)22, with unit-call parameters a = b = 67.14, c = 266.77 A
-
17beta-HSD14 in ternary complex with NADP+ and estradiol, modelling
-
active site analysis of 17beta-hydroxysteroid dehydrogenase type 1 enzyme complexes (estradiol/NADP+, equilin/NADP+, dehydroepiandrosterone) using the SPROUT program
crystal structure of 17beta-HSD1 complexed with testosterone or estradiol are shown. Both testosterone and estradiol bind in the narrow hydrophobic tunnel of 17beta-HSD1 with a high degree of complementarity. Testosterone is bound in an alternative orientation to 17beta-HSD1 compared with estradiol. Residue L149 plays an important role in the discrimination between C19 androgen and C18 estrogen
-
crystallization and crystal structure of the complex of the enzyme with the dual-site inhibitor, EM-139
-
hanging drop vapor diffusion method
hanging-drop vapour diffusion method at 27°C, binary and ternary crystal structures of the enzyme complexed with estrone and NADP+, crystals in this study belonged to the space group P212121 and contain a dimer per asymmetric unit
hanging-drop vapour diffusion method at 27°C, crystallization of the enzyme in complex with estrone and NADP+. His221 is the key residue responsible for the reorganization and stabilization of the reversely bound estrone, leading to the formation of a dead end complex, which exists widely in NADP(H)-preferred enzymes for the regulation of their enzymatic activity
in complex with ligands estradiol, equiline, 5-alpha-dihydrotestosterone, O5'-[9-(3,17beta-dihydroxy-1,3,5(10)-estratrien-16beta-yl)nonanoyl]adenosine and 3-[[(16beta,17beta)-3,17-dihydroxyestra-1,3,5(10)trien-16-yl]methyl]benzamide. Construction of pharmacophore model
method for crystallization of a labile enzyme
-
ternary complex of the 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one and NADP+
the purified enzyme variants T205 and S205 in apoform, as holoenzyme, or in complex with estrone or inhibitor [6-(3,4-dihydroxyphenyl)pyridin-2-yl]-(4-fluoro-3-hydroxyphenyl)methanone, ternary complex enzyme-cofactor-inhibitor, X-ray diffraction structure determination and analysis at 1.52-2.02 A resolution