A novel 17 beta-hydroxysteroid dehydrogenase in Rhodococcus sp P14 for transforming 17 beta-estradiol to estrone

作者：Ye, Xueying; Wang, Hui; Kan, Jie; Li, Jin; Huang, Tongwang^*; Xiong, Guangming; Hu, Zhong^*

来源：Chemico-Biological Interactions, 2017, 276: 105-112.

DOI：10.1016/j.cbi.2017.06.010

• 17 beta-hydroxysteroid dehydrogenases (17 beta-HSD)
• Estradiol
• Rhodococcus sp P14
• Bacterium
• Degradation

17 beta-hydroxysteroid dehydrogenases (17 beta-HSD) are a group of oxidoreductase enzymes that exhibit high specificity for 17C reduction/oxidation. However, the mechanism of 17 beta-HSD in oxidizing steroid hormone 17 beta-estradiol to estrone in bacterium is still unclear. In this work, a functional bacterium Rhodococcus sp. P14 was identified having rapid ability to oxidize estradiol into estrone in mineral salt medium (MSM) within 6 h. The functional genes encoding NADH-dependent oxidoreductase were successfully detected with the help of bioinformatics, and it was identified that it contained two consensus regions affiliated to the short-chain dehydrogenase/reductase (SDR) superfamily. Expression of 17 beta-HSD could be induced by estradiol in strain P14. The 17 beta-HSD gene from Rhodococcus sp. P14 was expressed in Escherichia coli strain BL21. Furthermore, recombinant 17b-HSD-expressing BL21 cells showed a high transformation rate, they are capable of transforming estradiol to estrone up to 94%. The purified His17 beta- HSD protein also exhibited high catalyzing efficiency. In conclusion, this study provides the first evidence that a novel 17 beta-HSD in Rhodococcus sp. P14 can catalyze the oxidation of estradiol.

• 出版日期2017-10-1
• 单位中国医科大学; 汕头大学