This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys. The conformation of these residues, compared to that of the NAD molecule, seems to be similar to that of the homologous enzymes. Thus, its catalytic mechanism must be similar to those of the homologous enzymes. According to the literature [37], type 1 of this enzyme (17-beta-hydroxysteroid dehydrogenase) (Swiss-prot;P14061) catalyzes the reduction of estrone to estradiol-17-beta, whereas type 11 (Swiss-prot;Q8NBQ5) catalyzes the oxidation/dehydrogenation of 5-alpha-androstanediol to androstrone.
17beta,20alpha-hydroxysteroid dehydrogenase
Human placental estradiol 17 beta-dehydrogenase: structural and catalytic changes during urea denaturation.
The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors.
Grenoble : Universite Joseph Fourier (Thesis)
Human Type I 17Beta-Hydroxysteroid Dehydrogenase: Site Directed Mutagenesis and X-Ray Crystallography Structure-Function Analysis.
NAD(P)+ analogues: tools for the investigation of the active site of oestradiol 17beta-dehydrogenase from human placenta.
Affinity labelling of the estradiol-17 beta dehydrogenase from human placenta with substrate analogs.
Steroid specificity in the stimulation of human endometrial estradiol dehydrogenase.
Spatial relationship of steroid and cofactor at the active site of human placental estradiol 17 beta-dehydrogenase.
Inactivation of human placental 17 beta-estradiol dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase with active site-directed 17 beta-propynyl-substituted progestin analogs.
Affinity labeling of arginyl residues at the catalytic region of estradiol 17 beta-dehydrogenase from human placenta by 16-oxoestrone.
Photochemical inactivation of human placental estradiol 17 beta-dehydrogenase in the presence of 2,3-butanedione.
Human placental estradiol 17 beta-dehydrogenase: sequence of a histidine-bearing peptide in the catalytic region.
Chemical modification of lysine residues at active-site of human placental estradiol 17 beta-dehydrogenase.
Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA.
Preparation of 14,15-secoestra-1,3,5(10)-trien-15-ynes, inhibitors of estradiol dehydrogenase.
Stereospecificity of hydrogen transfer between progesterone and cofactor by human placental estradiol-17 beta dehydrogenase.
Hydrogen bonding in steroidogenesis: studies on new heterocyclic analogs of estrone that inhibit human estradiol 17 beta-dehydrogenase.
Estradiol 17 beta-dehydrogenase: full enzymatic activity in the absence of zinc.
Molecular cloning and amino acid sequence of the porcine 17 beta-estradiol dehydrogenase.
X-RAY CRYSTALLOGRAPHY (2.2 AND 1.7 ANGSTROMS).
Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution.
Studies on the three-dimensional structure of estrogenic 17 beta-hydroxysteroid dehydrogenase.
Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol.
Characterization of structural and functional properties of human 17 beta-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site-directed mutagenesis.
Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase.
3D-structure of human estrogenic 17beta-HSD1: binding with various steroids.
Crystallization and preliminary crystal structure of the complex of 17beta-hydroxysteroid dehydrogenase with a dual-site inhibitor.
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+.
17Beta-hydroxysteroid dehydrogenase from Cochliobolus lunatus: model structure and substrate specificity.
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 38-327, AND MUTAGENESIS OF LEU-149.
Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain.
Structure-based phylogenetic analysis of short-chain alcohol dehydrogenases and reclassification of the 17beta-hydroxysteroid dehydrogenase family.
Critical residues for the specificity of cofactors and substrates in human estrogenic 17beta-hydroxysteroid dehydrogenase 1: variants designed from the three-dimensional structure of the enzyme.
Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition.
A concerted, rational design of type 1 17beta-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity.
17-beta-Hydroxysteroid dehydrogenase type 1: computational design of active site inhibitors targeted to the Rossmann fold.
Pseudo-symmetry of C19 steroids, alternative binding orientations, and multispecificity in human estrogenic 17beta-hydroxysteroid dehydrogenase.
The derivation of a potential transition state for the reduction reaction catalysed by 17beta-hydroxysteroid dehydrogenase--an approximate representation of its active site for use in drug design and discovery.
Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation.
Structure and function of human 17beta-hydroxysteroid dehydrogenases.
Binary and ternary crystal structure analyses of a novel inhibitor with 17beta-HSD type 1: a lead compound for breast cancer therapy.
17beta-hydroxysteroid dehydrogenase type 1 stimulates breast cancer by dihydrotestosterone inactivation in addition to estradiol production.