Production of bioactive 3'-hydroxy-stilbene compounds by using flavin-dependent monooxygenase, Sam5

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Title
Production of bioactive 3'-hydroxy-stilbene compounds by using flavin-dependent monooxygenase, Sam5
Author(s)
Kyung Taek Heo; Byungsan Lee; Sangkeun Son; Jong Seog AhnJae-Hyuk JangYoung-Soo Hong
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 28, no. 7, pp. 1105-1111
Publication Year
2018
Abstract
The flavin-dependent monooxygenase Sam5 was previously reported to be a bifunctional hydroxylase with a coumarte 3-hydroxylase and a resveratrol 3'-hydroxylase activity. In this article, we showed the Sam5 enzyme has 3'-hydroxylation activities for methylated resveratrol (pinostilbene and pterostilbene), hydroxylated resveratrol (oxyresveratrol) and glycosylated resveratrol (piceid) as substrates. However, the use of piceid, a glycone type stilbene, as a substrate for bioconversion experiments with the Sam5 enzyme expressed in, Escherichia coli does not convert to the hydroxylated compound astringin, but it has converted in vitro enzyme reactions. Finally, we report a novel catalytic activity of Sam5 monooxygenase for the synthesis of piceatannol derivatives, 3'-hydroxylated stilbene compounds. Development of this bioproduction method for the hydroxylation of stilbenes is challenging because of the difficulty in expressing P450-type hydroxylase in E. coli and regionspecific chemical synthesis.
Keyword
MonooxygenaseSam5hydroxy-stilbenepiceatannol
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.4014/jmb.1804.04007
Type
Article
Appears in Collections:
Ochang Branch Institute > Anticancer Agent Research Center > 1. Journal Articles
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