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.
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TL;DR: Rat ovarian 20α-hydroxysteroid dehydrogenase was purified 230-fold with a 48% recovery through a 3-step process involving hydrophobic, gel filtration and gree dye affinity chromatography, indicating a sequential mechanism for the enzyme.
14 citations
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TL;DR: An AKR-dependent whole-cell biotransformation process that can be used for production of human AKR metabolites on a large scale is established.
14 citations
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TL;DR: The 3-hydroxy-13β-D-secooxime has an IC50 value of 0.070 μM and is one of the most effective 17β-HSD1 inhibitors reported to date in the literature, i.e. more efficient inhibition in the presence of NADH than NADPH.
Abstract: The inhibitory effects of 13-epimeric estrones, D-secooxime and D-secoalcohol estrone compounds on human placental 17β-hydroxysteroid dehydrogenase type 1 isozyme (17β-HSD1) were investigated. The transformation of estrone to 17β-estradiol was studied by an in vitro radiosubstrate incubation method. 13α-Estrone inhibited the enzyme activity effectively with an IC50 value of 1.2 μM, which indicates that enzyme affinity is similar to that of the natural estrone substrate. The 13β derivatives and the compounds bearing a 3-hydroxy group generally exerted stronger inhibition than the 13α and 3-ether counterparts. The 3-hydroxy-13β-D-secoalcohol and the 3-hydroxy-13α-D-secooxime displayed an outstanding cofactor dependence, i.e. more efficient inhibition in the presence of NADH than NADPH. The 3-hydroxy-13β-D-secooxime has an IC50 value of 0.070 μM and is one of the most effective 17β-HSD1 inhibitors reported to date in the literature.
14 citations
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TL;DR: Models of the enzyme-inhibitor complexes suggest that Tyr118 and Phe311 are important residues for inhibitor recognition and orientation in the active site of AKR1C21.
14 citations
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11 Apr 2007
TL;DR: In this paper, a process for the enantioselective enzymatic reduction of compounds which have a steroid structure (ABCD), including one or more heteroatoms and/or an aromatic in the ring structure, is described.
Abstract: A process for the enantioselective enzymatic reduction of compounds which have a steroid structure (ABCD), including one or more heteroatoms, one or more double bonds and/or an aromatic in the ring structure and which have at least one oxo group at position 3, 7, 11, 12 or 17 of the steroid ring system or in α-position at any carbon radical on the steroid skeleton (= oxosteroid compound/hydroxysteroid compound), where the oxosteroid compound is reduced with a hydroxysteroid dehydrogenase in the presence of a cofactor NADH or NADPH is characterized in that a) the oxosteroid compound is present in the reaction mixture in a concentration of >50 g/l, b) the oxidized cofactor NAD or NADP which is formed by the hydroxysteroid dehydrogenase is regenerated continuously by oxidation of a secondary alcohol of the general formula RxRyCHOH where Rx, Ry independently of one another represent hydrogen, branched or unbranched Cl-C8-alkyl and Ctotal ≥3, or by oxidation of a C4-C6-cycloalkanol, and c) an additional oxidoreductase/alcohol dehydrogenase is employed for oxidizing the secondary alcohol of the general formula RXRYCHOH or of the cycloalkanol.
14 citations