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17Beta-hydroxysteroid dehydrogenase activity in Streptomyces hydrogenans
Acta Microbiologica Academiae Scientiarum Hungaricae
|January 1, 1975
Summary
Streptomyces hydrogenans efficiently converts testosterone to androstenedione. The study identified and characterized the 17beta-hydroxysteroid dehydrogenase enzyme responsible for this biotransformation.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Steroid biotransformation is crucial in pharmaceutical and chemical industries.
- Streptomyces species are known for their metabolic versatility in converting steroids.
Purpose of the Study:
- To investigate the biotransformation of testosterone to androstenedione by Streptomyces hydrogenans.
- To identify and characterize the enzyme responsible for this conversion.
Main Methods:
- In vivo studies of steroid conversion, uptake, and release.
- Thin-layer chromatography and recrystallization for steroid analysis.
- Enzyme isolation via sonification and gel filtration (Sephadex G-200).
Main Results:
- Streptomyces hydrogenans efficiently converts testosterone to androstenedione.
- The 17beta-hydroxysteroid dehydrogenase activity was localized in the soluble fraction and enriched.
- The enzyme requires NAD+ as a cofactor and exhibits photometric activity.
- Enzyme activity increased when S. hydrogenans was cultured with testosterone, estradiol, or 5alphaH-dihydrotestosterone.
Conclusions:
- Streptomyces hydrogenans possesses a potent 17beta-hydroxysteroid dehydrogenase for testosterone biotransformation.
- The enzyme's activity is inducible by androgens and estrogens.
- This enzyme is a promising candidate for biotechnological applications in steroid modification.