53-42-9Relevant articles and documents
An Easy Determination of Epimeric Androsterones by Collision Spectroscopy: the Molar Ratio of 5β-androstan-3α-ol-17-one and 5β-androstan-3β-ol-17-one Obtained by Hydrogenation of 5β-androstan-3,17-dione on Cu/Al2O3
Pelli, Beatrice,Traldi, Pietro,Gargano, Michele,Ravasio, Nicoletta,Rossi, Michele
, p. 183 - 185 (1987)
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Stereo selective one-step reduction in the steroid skeleton 4 - ene -3 - ketone as a 3 α - hydroxy - 5 β - hydrogen A/B cis structure method
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Paragraph 0022; 0041; 0042; 0043, (2017/02/17)
The invention relates to a method for one-step reduction of a 4-ene-3-one structure in a steroid skeleton into an A/B cis-3a-hydroxy-5b-hydrogen structure, belonging to the fields of organic chemistry and drug synthesis. According to the method, under the conditions of room temperature and an environment of absolute ethyl alcohol, cuprous chloride is used as a catalyst and sodium borohydride is used as a reducing agent for high-selectivity conversion of the 4-ene-3-one structure of 4-AD, ADD and derivatives thereof into the A/B cis-3a-hydroxy-5b-hydrogen structure. According to results of X-diffraction results, an androstane-3a-hydroxy-5b-hydrogen-17-one product prepared by using the method has a stereo structure; reaction conditions are mild and simple; used reagents are cheap and easily available; operation is convenient; good repeatability is realized, and high yield is obtained. The method provided by the invention lays a good foundation for exploitation of resourceful utilization of sterol and for research on synthesis of drugs like ursodesoxycholic acid, chenodeoxycholic acid, deoxycholic acid and ecdyson with the A/B cis-structure with non-cholic acid type steroids as raw materials.
Substrate specificity of a mouse aldo-keto reductase (AKR1C12)
Endo, Satoshi,Matsumoto, Kengo,Matsunaga, Toshiyuki,Ishikura, Shuhei,Tajima, Kazuo,El-Kabbani, Ossama,Hara, Akira
, p. 2488 - 2492 (2007/10/03)
AKR1C12, a mouse member of the aldo-keto reductase (AKR) superfamily, is highly expressed in the stomach and is identical to a protein encoded in an interleukin-3-regulated gene in mouse myeloid cells, but its function remains unknown. In this study, the recombinant AKR1C12 was purified to homogeneity and the specificity for coenzymes and substrates was examined at a physiological pH of 7.4. The enzyme reduced various α-dicarbonyl compounds, several ketosteroids, aldehydes and some ketones using NADH as the preferred coenzyme. In the reverse reaction, the enzyme showed coenzyme preference for NAD +, and oxidized 3α-, 17β- and 20α-hydroxysteroids, and non-steroidal aliphatic and alicyclic alcohols, of which many hydroxysteroids and geranylgeraniol were good substrates, exhibiting low K m and high kcat/Km values. The results, together with the intracellular high ratio of NAD+/NADH, suggest that AKR1C12 functions as a dehydrogenase for the endogenous hydroxysteroids and geranylgeraniol in mouse stomach and myeloid cells.
