Topic
Hydroxysteroid dehydrogenase
About: Hydroxysteroid dehydrogenase is a research topic. Over the lifetime, 1087 publications have been published within this topic receiving 28468 citations. The topic is also known as: hydroxysteroid dehydrogenase.
Papers published on a yearly basis
Papers
More filters
TL;DR: Kinetic analysis and molecular-modelling studies of 17alpha- and 17beta-hydroxysteroid substrates in the active site of AKR1C21 suggested that Gly225 and Gly226 play an important role in determining the substrate stereospecificity of the enzyme, and it is shown that these residues are critical for the binding of substrates.
Abstract: 3(17)alpha-Hydroxysteroid dehydrogenase (AKR1C21) is a unique member of the aldo-keto reductase (AKR) superfamily owing to its ability to reduce 17-ketosteroids to 17alpha-hydroxysteroids, as opposed to other members of the AKR family, which can only produce 17beta-hydroxysteroids. In this paper, the crystal structure of a double mutant (G225P/G226P) of AKR1C21 in complex with the coenzyme NADP(+) and the inhibitor hexoestrol refined at 2.1 A resolution is presented. Kinetic analysis and molecular-modelling studies of 17alpha- and 17beta-hydroxysteroid substrates in the active site of AKR1C21 suggested that Gly225 and Gly226 play an important role in determining the substrate stereospecificity of the enzyme. Additionally, the G225P/G226P mutation of the enzyme reduced the affinity (K(m)) for both 3alpha- and 17alpha-hydroxysteroid substrates by up to 160-fold, indicating that these residues are critical for the binding of substrates.
4 citations
TL;DR: A 2.5-fold increase of specific activity was obtained during solubilization under optimal conditions and the soluble fraction contained more than 90% of the enzymatic activity.
4 citations
TL;DR: Clinical and biochemical features in a 13-year-old 46, XY individual who presented with progressive pubertal virilization are described.
4 citations
TL;DR: In vivo, 20beta-hydroxysteroid dehydrogenase appears to consist of four equal subunits, and the monomers, molecular weight of 27 300, show a high tendency to form dimers and tetramers in the absence of dissociating agents.
Abstract: Antiserum against crystallized 20beta-hydroxysteroid dehydrogenase from Streptomyces hydrogenans was used for various immunodiffusion and immunoprecipitation tests to show an increase of the de novo synthesis of 20beta-hydroxysteroid dehydrogenase by Streptomyces hydrogenans after cultivation of the cells in the presence of 11beta,21-dihydroxy-4,17(20)-pregnadien-3-one. Half lives of mRNA for 20beta-hydroxysteroid dehydrogenase in induced cells and of total mRNA in non-induced cells were calculated to be 126 s and 66 s, respectively. In vivo, 20beta-hydroxysteroid dehydrogenase appears to consist of four equal subunits. The monomers, molecular weight of 27 300, show a high tendency to form dimers and tetramers in the absence of dissociating agents. The aggregation is completely reversible in the presence of increasing concentrations of sodium dodecylsulfate.
4 citations
TL;DR: The effect of estradiol, hydrocortisone and progesterone on 3α,20β- and 3β,17β-hydroxysteroid dehydrogenase (HSD) in mutants of Streptomyces hydrogenans was compared to the steroid response of the wild type.
Abstract: The effect of estradiol, hydrocortisone and progesterone on 3α,20β-and 3β,17β-hydroxysteroid dehydrogenase (HSD) in mutants of Streptomyces hydrogenans was compared to the steroid response of the wild type. Mutants were defective in arginine biosynthesis and/or aerial mycelial formation and lacked both enzymes or only 17β-HSD. Some 17β-HSD mutants had lost the ability to be induced by estradiol, by progesterone or by both. Some 20β-HSD mutants had lost the ability to be induced by hydrocortisone, by progesterone or by both. Non-inducibility of 17β-and 20β-HSD by progesterone was not co-ordinate. An additional study of the growth phase-dependent enzyme activity of the wild type after induction with estradiol, hydrocortisone and progesterone was performed.
4 citations