1-Ene-steroid reductase of Mycobacterium SP. NRRL B-3805

Goren, Tamar; Harnik, M.; Rimon, Sara; Aharonowitz, Yair

doi:10.1016/0022-4731(83)90361-8

Cited by 18 publications

(12 citation statements)

References 16 publications

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“…The results evidenced membrane-bound and soluble forms of 17␤-OH SDH in sterol-transforming mycobacteria similar to those reported for other organisms [6][7][8].…”

Section: Discussionsupporting

confidence: 52%

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

Egorova

Nikolayeva

Suzina

et al. 2005

The Journal of Steroid Biochemistry and Molecular Biology

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“…The results evidenced membrane-bound and soluble forms of 17␤-OH SDH in sterol-transforming mycobacteria similar to those reported for other organisms [6][7][8].…”

Section: Discussionsupporting

confidence: 52%

“…NRRL B-3805, were found to account for 17-keto-1(2)-dehydro steroid bioconversion. The former activity was detected in the soluble cell fraction, whereas the latter was associated with the insoluble fraction [8].…”

Section: Introductionmentioning

confidence: 95%

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

Egorova

Nikolayeva

Suzina

et al. 2005

The Journal of Steroid Biochemistry and Molecular Biology

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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%

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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“…Alternative explanations are that either regulatory mechanisms or the presence of a 1‐ene‐steroid reductase activity, as found in Mycobacterium sp. (Goren et al , 1983), prevents complete conversion of AD into ADD.…”

Section: Resultsmentioning

confidence: 99%

Molecular and functional characterization of kshA and kshB, encoding two components of 3‐ketosteroid 9α‐hydroxylase, a class IA monooxygenase, in Rhodococcus erythropolis strain SQ1

Geize

Hessels

Gerwen

et al. 2002

Molecular Microbiology

112

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Summary9a-Hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD) is catalysed by 3-ketosteroid 9a-hydroxylase (KSH), a key enzyme in microbial steroid catabolism. Very limited knowledge is presently available on the KSH enzyme. Here, we report for the first time the identification and molecular characterization of genes encoding KSH activity. The kshA and kshB genes, encoding KSH in Rhodococcus erythropolis strain SQ1, were cloned by functional complementation of mutant strains blocked in AD(D) 9a-hydroxylation. Analysis of the deduced amino acid sequences of kshA and kshB showed that they contain domains typically conserved in class IA terminal oxygenases and class IA oxygenase reductases respectively. By definition, class IA oxygenases are made up of two components, thus classifying the KSH enzyme system in R. erythropolis strain SQ1 as a two-component class IA monooxygenase composed of KshA and KshB. Unmarked in frame gene deletion mutants of parent strain R. erythropolis SQ1, designated strains RG2 (kshA mutant) and RG4 (kshB mutant), were unable to grow on steroid substrates AD(D), whereas growth on 9a-hydroxy-4-androstene-3,17-dione (9OHAD) was not affected. Incubation of these mutant strains with AD resulted in the accumulation of ADD (30-50% conversion), confirming the involvement of KshA and KshB in AD(D) 9a-hydroxylation. Strain RG4 was also impaired in sterol degradation, suggesting a dual role for KshB in both sterol and steroid degradation.

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1-Ene-steroid reductase of Mycobacterium SP. NRRL B-3805

Cited by 18 publications

References 16 publications

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

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

Engineering Mycobacterium smegmatis for testosterone production

Molecular and functional characterization of kshA and kshB, encoding two components of 3‐ketosteroid 9α‐hydroxylase, a class IA monooxygenase, in Rhodococcus erythropolis strain SQ1

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