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The effect of 3-ketosteroid- Delta super(1)-dehydrogenase isoenzymes on the transformation of AD to 9 alpha -OH-AD by Rhodococcus rhodochrous DSM43269

Rhodococcus rhodochrous DSM43269 is well known for its 3-ketosteroid-9 alpha -hydroxylases. However, the function of its 3-ketosteroid- Delta super(1)-dehydrogenases (KSDD) remains unknown. This study compared the involvement of ksdds in the strain's androst-4-ene-3,17-dione (AD) transformation...

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Published in:Journal of industrial microbiology & biotechnology 2016-09, Vol.43 (9), p.1303-1311
Main Authors: Liu, Yang, Shen, Yanbing, Qiao, Yuqian, Su, Liqiu, Li, Can, Wang, Min
Format: Article
Language:English
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Summary:Rhodococcus rhodochrous DSM43269 is well known for its 3-ketosteroid-9 alpha -hydroxylases. However, the function of its 3-ketosteroid- Delta super(1)-dehydrogenases (KSDD) remains unknown. This study compared the involvement of ksdds in the strain's androst-4-ene-3,17-dione (AD) transformation via gene deletion. The conversion was performed using AD as substrate or directly with 9 alpha -hydroxyandrost-4-ene-3,17-dione (9 alpha -OH-AD). The single deletion of ksdd1 or ksdd3 did not appear to result in the accumulation of 9 alpha -OH-AD, whereas the single mutant ksdd2 could preserve this compound to some extent. To further compare the role of ksdds in this strain, double mutants were constructed. All ksdd2 mutants combined with ksdd1 and/or ksdd3 resulted in the accumulation of 9 alpha -OH-AD, among which the double mutant ksdd2,3 behaved similarly to the single mutant ksdd2 in this process. The mutant that lacked both ksdd1 and ksdd3 was still displayed, with no effect on the degradation of 9 alpha -OH-AD. The triple mutant ksdd1,2,3 was then constructed and exhibited the same capability as ksdd1,2, accumulating more 9 alpha -OH-AD than ksdd2,3 and ksdd2. The transcription of KSDD1 and KSDD2 increased, whereas that of KSDD3 seemed to exhibit no change, despite the use of the inducer AD or 9 alpha -OH-AD. Thus, only ksdd1 and ksdd2 were involved in the transformation of AD to 9 alpha -OH-AD. ksdd2 had the main role, ksdd1 had a minor effect on 9 alpha -OH-AD degradation, and ksdd3 did not exhibit any action in this course.
ISSN:1367-5435
1476-5535
DOI:10.1007/s10295-016-1804-0