Exploration of the Glycosyltransferase BmmGT1 from a Marine-Derived Bacillus Strain as a Potential Enzyme Tool for Compound Glycol-Diversification

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.