Exploration of the Glycosyltransferase BmmGT1 from a MarineDerived Bacillus Strain as a Potential Enzyme Tool for Compound Glycol-Diversification
2018
Quanquan Liu, Ocean University of China, Qingdao, China | Pengfei Ren, Ocean University of China, Qingdao, China | Yang Liu, Ocean University of China, Qingdao, China | Wen Qin, Ocean University of China, Qingdao, China | Huayue Li, Ocean University of China, Qingdao, China | Wenli Li, Ocean University of China, Qingdao, China
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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