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- W2010297573 abstract "1. β-Hydroxysteroid dehydrogenase (3 (or 17)-β-hydroxysteroid: NAD(P) oxidoreductase, EC. 1.1.1.51) was prepared from Pseudomonas testosteroni. This enzyme obeyed first-order kinetics with androst-4-ene-3,17-dione as substrate between 1.0·10−4 and 2.5·10−6 M. 2. The most effective inhibitors, with the concentration at which they inhibited 50%, were: 2-hydroxymethylene-17α-methylandrostan-17β-ol-3-one (9·10−7 M), 2α-cyano-4,4,17α-trimethylandrost-5-en-17β-ol-3-one (8·10−7 M), 17β-hydroxy-4,4,17α-trimethylandrost-5-enol[3,2-c]pyrazole (8·10−7M), and 4,4-dimethyl-17β-hydroxyandrost-5-eno[3,2-c]pyrzole (8·10−7 M). Testosterone inhibited 50% at 2·10−5 M. 3. A study of 42 derivatives of the androstane nucleus showed that the degree of inhibition depended upon the nature of the substituents on positions 2, 3, 4 and 17 of the steroid nucleus. Spacial presentation of these groups to the enzyme by the arrangement of double bonds or by their absence also affected inhibition." @default.
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- W2010297573 title "Inhibition of β-hydroxysteroid dehydrogenase I. Structural characteristics of some steroidal inhibitors" @default.
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- W2010297573 doi "https://doi.org/10.1016/0006-3002(63)90510-9" @default.
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