Localization of 17β-hydroxysteroid dehydrogenase in Mycobacterium sp. VKM Ac-1815D mutant strain

Egorova, Olga V.; Nikolayeva, Vera M.; Suzina, N. E.; Donova, Marina V.

doi:10.1016/j.jsbmb.2004.12.044

Cited by 9 publications

(7 citation statements)

References 20 publications

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“…The intracellular presence of this enzyme has been described in a mutant strain of Mycobacterium sp. (Egorova et al 2005), and an extracellular 3␤-HSD form was found in Mycobacterium vaccae by Nikolayeva et al (2004). The synthesis of Adiol found in our study also suggests the presence of a 17␤-OH-steroid dehydrogenase like in M. smegmatis.…”

Section: Discussionsupporting

confidence: 73%

Mycobacterium smegmatissynthesizes in vitro androgens and estrogens from different steroid precursors

et al. 2015

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Fast-growing mycobacteria such as Mycobacterium sp. and Mycobacterium smegmatis degrade natural sterols. They are a model to study tuberculosis. Interestingly, M. smegmatis has been found in river effluents derived from paper production, and therefore, it would be important to gain further insight into its capacity to synthesize steroids that are potential endocrine disruptors affecting the development and reproduction of fishes. To our knowledge, the capacity of M. smegmatis to synthesize estrogens and even testosterone has not been previously reported. Therefore, the objective of this study was to investigate the capacity of M. smegmatis to synthesize in vitro testosterone and estrogens from tritiated precursors and to investigate the metabolic pathways involved. Results obtained by thin-layer chromatography showed that (3)H-progesterone was transformed to 17OH-progesterone, androstenedione, testosterone, estrone, and estradiol after 6, 12, or 24 h of incubation. (3)H-androstenedione was transformed into testosterone and estrogens, mainly estrone, and (3)H-testosterone was transformed to estrone and androstenedione. Incubation with (3)H-dehydroepiandrosterone rendered androstenediol, testosterone, and estrogens. This ability to transform less potent sex steroids like androstenedione and estrone into other more active steroids like testosterone and estradiol or vice versa suggests that M. smegmatis can influence the amount of self-synthesized strong androgens and estrogens and can transform those found in the environment.

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Section: Discussionsupporting

confidence: 73%

Mycobacterium smegmatissynthesizes in vitro androgens and estrogens from different steroid precursors

et al. 2015

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“…As the genes encoding 17β‐HSD enzymes from mycobacterial species have not been identified and these proteins have been only partially purified and characterized (Goren et al ., 1983; Egorova et al ., 2002a, 2005), we initially selected as enzyme candidates for metabolic engineering the well‐described 17β‐HSDs from the bacterium C. testosteroni (Schultz et al ., 1977; Lefebvre et al .,1979; Minard et al ., 1985 ; Genti‐Raimondi et al ., 1991; Yin et al ., 1991; Abalain et al ., 1993; Benach et al ., 1996, 2002; Oppermann et al ., 1997; Cabrera et al ., 2000) and the fungus C. lunatus (Plemenitas et al ., 1988; Rižner et al ., 1996, 1999, 2000, 2001a,b; Rižner and Zakelj‐Mavric, 2000; Zorko et al ., 2000; Kristan et al ., 2003, 2005, 2007a,b; Cassetta et al ., 2005; Ulrih and Lanisnik Rižner, 2006; Brunskole et al ., 2009; Svegelj et al ., 2012), because both enzymes present some relevant differences. Although they catalyse a reversible reaction and display similar reaction mechanisms, the reaction equilibrium of the fungal 17β‐HSD is shifted towards reduction, whereas the bacterial enzyme is shifted towards oxidation, as this enzyme is mainly involved into the TS catabolism in C. testosteroni (Genti‐Raimondi et al., 1990; Cabrera et al ., 2000).…”

Section: Resultsmentioning

confidence: 99%

“…On the other hand, enzymatic reduction of AD to TS by 17β‐HSD has also been described in different microorganisms (Donova et al ., 2005), including bacteria (Schultz et al ., 1977; Payne and Talalay, 1985; Sarmah et al ., 1989; Liu et al ., 1994; Egorova et al ., 2002a,b, 2005), yeasts (Ward and Young, 1990; Singer et al ., 1991; Długoński and Wilmańska, 1998; Pajic et al ., 1999), filamentous fungi (Kristan and Rižner, 2012) and plants (Hamada and Kawabe, 1991). Moreover, a single‐step microbial transformation process has been reported for the production of TS from sterols using several Mycobacterium sp.…”

Section: Introductionmentioning

confidence: 99%

Engineering Mycobacterium smegmatis for testosterone production

Fernández-Cabezón

Galán

2016

Microbial Biotechnology

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SummaryA new biotechnological process for the production of testosterone (TS) has been developed to turn the model strain Mycobacterium smegmatis suitable for TS production to compete with the current chemical synthesis procedures. We have cloned and overexpressed two genes encoding microbial 17β‐hydroxysteroid: NADP 17‐oxidoreductase, from the bacterium Comamonas testosteroni and from the fungus Cochliobolus lunatus. The host strains were M. smegmatis wild type and a genetic engineered androst‐4‐ene‐3,17‐dione (AD) producing mutant. The performances of the four recombinant bacterial strains have been tested both in growing and resting‐cell conditions using natural sterols and AD as substrates respectively. These strains were able to produce TS from sterols or AD with high yields. This work represents a proof of concept of the possibilities that offers this model bacterium for the production of pharmaceutical steroids using metabolic engineering approaches.

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“…The enzymes catalysing the same dehydrogenation reaction in oxic steroid catabolism have been isolated and characterized from several species of bacteria, such as Alcaligenes sp., C. testosteroni and Mycobacterium sp. (Groman & Engel, 1977;Payne & Talalay, 1985;Egorova et al, 2005). All of them belong to the SDR protein family and have the highest dehydrogenation activity under alkaline conditions (pH 8-9).…”

Section: Discussionmentioning

confidence: 99%

Initial steps in anoxic testosterone degradation by Steroidobacter denitrificans

et al. 2010

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Steroid compounds have many important physiological activities in higher organisms. Testosterone and related steroids are important environmental contaminants that disrupt the endocrine systems of animals. The degradation of steroids, especially under anoxic conditions, is challenging because of their complex chemical structure. A denitrifying c-proteobacterium, Steroidobacter denitrificans, able to grow anaerobically on a variety of steroids as the sole carbon and energy source was adopted as a model organism to study the anoxic degradation of testosterone. We identified the initial intermediates involved in the anoxic testosterone degradation pathway of S. denitrificans. We demonstrated that under anoxic conditions, S. denitrificans initially oxidizes testosterone to 1-dehydrotestosterone, which is then transformed to androsta-1,4-diene-3,17-dione. In addition, it seems that androst-4-en-3,17-dione can also be directly produced from testosterone by S. denitrificans cells. In general, the initial steps of anoxic testosterone degradation by S. denitrificans are similar to those of the oxic pathway demonstrated in Comamonas testosteroni.

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Localization of 17β-hydroxysteroid dehydrogenase in Mycobacterium sp. VKM Ac-1815D mutant strain

Cited by 9 publications

References 20 publications

Mycobacterium smegmatissynthesizes in vitro androgens and estrogens from different steroid precursors

Mycobacterium smegmatissynthesizes in vitro androgens and estrogens from different steroid precursors

Engineering Mycobacterium smegmatis for testosterone production

Initial steps in anoxic testosterone degradation by Steroidobacter denitrificans

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