Identification of cholesterol oxidase from fast-growing mycobacterial strains and Rhodococcus sp.

Wilmańska, Danuta; Dziadek, Jarosław; Sajduda, Anna; Milczarek, Krystyna; Jaworski, Adam; Murooka, Yoshikatsu

doi:10.1016/0922-338x(95)94077-5

Cited by 24 publications

(16 citation statements)

References 20 publications

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“…The data on the enzyme responsible for oxidation of sterol 3-OH-function in fast-growing mycobacteria are scarce [13,14]. The ChO from M. fortuitum, M. vaccae, M. phlei, M. smegmatis were localized intracellularly [14].…”

Section: Introductionmentioning

confidence: 98%

Extracellular 3β-hydroxysteroid oxidase of Mycobacterium vaccae VKM Ac-1815D

Nikolayeva

Egorova

Dovbnya

et al. 2004

The Journal of Steroid Biochemistry and Molecular Biology

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Section: Introductionmentioning

confidence: 98%

Extracellular 3β-hydroxysteroid oxidase of Mycobacterium vaccae VKM Ac-1815D

Nikolayeva

Egorova

Dovbnya

et al. 2004

The Journal of Steroid Biochemistry and Molecular Biology

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“…The disruption of both genes was required to block effectively the AD degradation process (Geize et al, 2002). Reported mycobacterial activities in sterol biodegradation (Wilmanska et al, 1995;Wovcha et al, 1979) are not supported by the identification and molecular characterization of genes involved in this process. Here we report on the identification of the main ksdD gene in Mycobacterium smegmatis and its characterization by unmarked gene deletion.…”

Section: Introductionmentioning

confidence: 99%

Identification and targeted disruption of the gene encoding the main 3-ketosteroid dehydrogenase in Mycobacterium smegmatis

et al. 2005

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The catabolic potential for sterol degradation of fast-growing mycobacteria is well known. However, no genes or enzymes responsible for the steroid degradation process have been identified as yet in these species. One of the key enzymes required for degradation of the steroid ring structure is 3-ketosteroid D 1 -dehydrogenase (KsdD). The recent annotation of the Mycobacterium smegmatis genome (TIGR database) revealed six KsdD homologues. Targeted disruption of the MSMEG5898 (ksdD-1) gene, but not the MSMEG4855 (ksdD-2) gene, resulted in partial inactivation of the cholesterol degradation pathway and accumulation of the intermediate 4-androstene-3,17-dione. This effect was reversible by the introduction of the wild-type ksdD-1 gene into M. smegmatis DksdD-1 or overexpression of ksdD-2. The data indicate that KsdD1 is the main KsdD in M. smegmatis, but that KsdD2 is able to perform the cholesterol degradation process when overproduced.

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“…The most common microbial sources for production of CHOx are mainly Arthrobacter [33,34], Bacillus sp. [12,35], Brevibacterium [36], Bordetella [37], [38,39], Nocardia [40,41], Rhodococcus [42,43] and Streptomyces [44][45][46]. Some Gramnegative bacteria such as Burkholderia [31], Chromobacterium [1] and Pseudomonas sp.…”

Section: Microbial Strains Producing Cholesterol Oxidasementioning

confidence: 99%