α类固醇脱氢酶
α类固醇脱氢酶结构式
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常用名 | α类固醇脱氢酶 | 英文名 | 3alpha-hydroxysteroid dehydrogenase |
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| CAS号 | 9028-56-2 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Electronic effects of para-substitution on acetophenones in the reaction of rat liver 3alpha-hydroxysteroid dehydrogenase.
Bioorg. Med. Chem. 16 , 1084-9, (2008) Stereoselective reductive metabolism of various p-substituted acetophenone derivatives was studied using isolated rat liver 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD). Kinetic experiments were performed and analyzed by measuring the products by HPLC usi... |
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Enzyme biosensor for androsterone based on 3α-hydroxysteroid dehydrogenase immobilized onto a carbon nanotubes/ionic liquid/NAD+ composite electrode.
Talanta 99 , 697-702, (2012) A 3α-hydrosteroid biosensor for androsterone determination has been prepared by immobilizing the enzyme 3α-hydroxysteroid dehydrogenase (3α-HSD) in a composite electrode platform constituted of a mixture of multi-walled carbon nanotubes (MWCNTs), octylpyridin... |
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Prostaglandin dehydrogenase activity of purified rat liver 3 alpha-hydroxysteroid dehydrogenase.
Biochem. Biophys. Res. Commun. 148(2) , 646-52, (1987) Homogeneous 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from rat liver cytosol displays 9, 11, and 15-hydroxyprostaglandin dehydrogenase activity. Using [14C]-PGF2 alpha as substrate the products of this reaction were separated by TLC and identified by... |
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Effects of gonadectomy on glucocorticoid metabolism in obese Zucker rats.
Endocrinology 148(10) , 4836-43, (2007) Glucocorticoids are metabolized by 11beta-hydroxysteroid dehydrogenase 1 (11betaHSD1) and the A-ring reductases (5alpha- and 5beta-reductases). Dysregulation of these enzymes has been reported in liver and adipose tissue in obese humans and animals, potential... |
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Cephalosporolides H and I, Two Novel Lactones from a Marine-Derived Fungus, Penicillium sp.
Arch. Pharm. Res. 30(7) , 812-5, (2007) Two novel lactones, Cephalosporolides H (1) and 1 (2), were isolated from the lyophilized culture broth of the marine-derived fungus, Penicillium sp. The structures were elucidated on the basis of extensive 1D- and 2D-NMR, as well as HRESI-MS spectroscopic an... |
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Understanding oligomerization in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: an in silico approach and evidence for an active protein.
J. Biotechnol. 129(1) , 131-9, (2007) 3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase (3alpha-HSD/CR) from Comamonas testosteroni belongs to the short chain dehydrogenase/reductase (SDR) protein superfamily and catalyzes the oxidoreduction of a variety of steroid substrates, including the ... |
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3alpha-Hydroxysteroid dehydrogenase type III deficiency: a novel mechanism for hirsutism.
J. Clin. Endocrinol. Metab. 93(4) , 1298-303, (2008) Dihydrotestosterone (DHT), the primary active androgen in peripheral target tissues, is metabolized by 3alpha-hydroxysteroid dehydrogenase type III (3alpha-HSD), encoded by the AKR1C2 gene, forming 5alpha-androstane-3alpha,17beta-diol (3alpha-diol). 3alpha-HS... |
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Allopregnanolone prevents memory impairment: effect on mRNA expression and enzymatic activity of hippocampal 3-α hydroxysteroid oxide-reductase.
Brain Res. Bull. 87(2-3) , 280-5, (2012) In this work we investigated how the neurosteroid allopregnanolone can modulate learning and memory processes. For this purpose, we used ovariectomized (OVX) rats subcutaneously injected with oestradiol benzoate (E) alone or E and progesterone (P). Then, rats... |
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Tissue distribution of human AKR1C3 and rat homolog in the adult genitourinary system.
J. Histochem. Cytochem. 56(9) , 853-61, (2008) Human aldo-keto reductase (AKR) 1C3 (type 2 3alpha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase) catalyzes androgen, estrogen, and prostaglandin metabolism. AKR1C3 is therefore implicated in regulating ligand access to the androgen ... |
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The Del1 deposition domain can immobilize 3alpha-hydroxysteroid dehydrogenase in the extracellular matrix without interfering with enzymatic activity.
Bioprocess Biosyst. Eng. 32(5) , 569-73, (2009) Developing methods that result in targeting of therapeutic molecules in gene therapies to target tissues has importance, as targeting can increase efficacy and decrease off target-side-effects. Work from my laboratory previously showed that the extracellular ... |