Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Exploration of the Glycosyltransferase BmmGT1 from a Marine-Derived Bacillus Strain as a Potential Enzyme Tool for Compound Glycol-Diversification

  • Liu, Quanquan (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China) ;
  • Ren, Pengfei (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China) ;
  • Liu, Yang (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China) ;
  • Qin, Wen (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China) ;
  • Li, Huayue (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China) ;
  • Li, Wenli (Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China)
  • Received : 2018.02.09
  • Accepted : 2018.03.29
  • Published : 2018.06.28
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Abstract

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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