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KMID : 0545120180280060931
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Journal of Microbiology and Biotechnology
2018 Volume.28 No. 6 p.931 ~ p.937
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Exploration of the Glycosyltransferase BmmGT1 from a Marine-Derived Bacillus Strain as a Potential Enzyme Tool for Compound Glycol-Diversification
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Liu Quanquan
Ren Pengfei
Liu Yang
Qin Wen
Li Huayue
Li Wenli
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Abstract
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Glycosyltransferases (GTs) from microbes are an emerging and rich source for efficient glycol-transformation of natural/unnatural compounds. Here, we probed the catalytic capability and substrate promiscuity of BmmGT1 from marine-derived Bacillus methylotrophicus B-9987. The regioselectivity of BmmGT1 on macrolactin A (1) was explored by optimization of the reaction conditions, in which a series of O-glycosylated macrolactins (1a-1e) were generated, including two new di/tri-O-glucosyl analogs (1b and 1e). Furthermore, BmmGT1 was able to catalyze the glycosylation of the thiol (S-) or amine (N-) sites of phenolic compounds (2 and 3), leading to the generation of N- (2a) or S-glycosides (3a and 3b). The present study demonstrates that BmmGT1 could serve as a potential enzyme tool for O-, N-, or S-glycosyl structural diversification of compounds for drug discovery.
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KEYWORD
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Glycosyltransferase, marine-derived Bacillus, aglycon promiscuity, glycol-diversification, macrolactin
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