Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Exploring the Nucleophilic N- and S-Glycosylation Capacity of Bacillus licheniformis YjiC Enzyme

  • Bashyal, Puspalata (Department of Life Science and Biochemical Engineering, Sun Moon University) ;
  • Thapa, Samir Bahadur (Department of Life Science and Biochemical Engineering, Sun Moon University) ;
  • Kim, Tae-Su (Department of Life Science and Biochemical Engineering, Sun Moon University) ;
  • Pandey, Ramesh Prasad (Department of Life Science and Biochemical Engineering, Sun Moon University) ;
  • Sohng, Jae Kyung (Department of Life Science and Biochemical Engineering, Sun Moon University)
  • Received : 2020.01.16
  • Accepted : 2020.03.15
  • Published : 2020.07.28
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Abstract

YjiC, a glycosyltransferase from Bacillus licheniformis, is a well-known versatile enzyme for glycosylation of diverse substrates. Although a number of O-glycosylated products have been produced using YjiC, no report has been updated for nucleophilic N-, S-, and C- glycosylation. Here, we report the additional functional capacity of YjiC for nucleophilic N- and S- glycosylation using a broad substrate spectrum including UDP-α-D-glucose, UDP-N-acetyl glucosamine, UDP-N-acetylgalactosamine, UDP-α-D-glucuronic acid, TDP-α-L-rhamnose, TDP-α-D-viosamine, and GDP-α-L-fucose as donor and various amine and thiol groups containing natural products as acceptor substrates. The results revealed YjiC as a promiscuous enzyme for conjugating diverse sugars at amine and thiol functional groups of small molecules applicable for generating glycofunctionalized chemical diversity libraries. The glycosylated products were analyzed using HPLC and LC/MS and compared with previous reports.

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References

  1. Kilcoyne M, Joshi L. 2007. Carbohydrates in therapeutics. Cardiovasc. Hematol. Agents Med. Chem. 5: 1876-1897.
  2. Kren V, Martinkova L. 2001. Glycosides in medicine: "The role of glycosidic residue in biological activity". Curr. Med. Chem. 8: 1303-1328. https://doi.org/10.2174/0929867013372193
  3. Kren V, Rezanka T. 2008. Sweet antibiotics - The role of glycosidic residues in antibiotic and antitumor activity and their randomization. FEMS Microbiol. Rev. 32: 858-889. https://doi.org/10.1111/j.1574-6976.2008.00124.x
  4. Wrodnigg TM, Sprenger F. 2004. Bioactive carbohydrates and recently discovered analogues as chemotherapeutics. Mini Rev. Med. Chem. 4: 437-459.
  5. Campbell JA, Davies GJ, Bulone V, Henrissat B. 1997. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326: 929-939. https://doi.org/10.1042/bj3260929u
  6. Coutinho PM, Deleury E, Davies GJ, Henrissat B. 2003. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328: 307-317. https://doi.org/10.1016/S0022-2836(03)00307-3
  7. Weymouth-Wilson AC. 1997. The role of carbohydrates in biologically active natural products. Nat. Prod. Rep. 14: 99-110. https://doi.org/10.1039/np9971400099
  8. Butler MS. 2004. The role of natural product chemistry in drug discovery. J. Nat. Prod. 67: 2141-2153. https://doi.org/10.1021/np040106y
  9. Xiao J, Muzashvili TS, Georgiev MI. 2014. Advances in the biotechnological glycosylation of valuable flavonoids. Biotechnol. Adv. 32: 1145-1156. https://doi.org/10.1016/j.biotechadv.2014.04.006
  10. Ko JH, Kim BG, Ahn JH. 2006. Glycosylation of flavonoids with a glycosyltransferase from Bacillus cereus. FEMS Microbiol. Lett. 258: 263-268. https://doi.org/10.1111/j.1574-6968.2006.00226.x
  11. Ahn BC, Kim BG, Jeon YM, Lee EJ, Lim Y, Ahn JH. 2009. Formation of flavone di-O-glucosides using a glycosyltransferase from Bacillus cereus. J. Microbiol. Biotechnol. 19: 387-390. https://doi.org/10.4014/jmb.0802.116
  12. Bashyal P, Pandey RP, Thapa SB, Kang MK, Kim CJ, Sohng JK. 2019. Biocatalytic synthesis of non-natural monoterpene O-glycosides exhibiting superior antibacterial and antinematodal properties. ACS Omega. 4: 9367-9375. https://doi.org/10.1021/acsomega.9b00535
  13. Thapa SB, Pandey RP, Bashyal P, Tokutaro Y, Sohng JK. 2019. Cascade biocatalysis systems for bioactive naringenin glucosides and quercetin rhamnoside production from sucrose. Appl. Microbiol. Biotechnol. 103: 8281-8281. https://doi.org/10.1007/s00253-019-10079-8
  14. Hultin P. 2005. Bioactive C-glycosides from bacterial secondary metabolism. Curr. Top. Med. Chem. 5: 1299-1331. https://doi.org/10.2174/156802605774643015
  15. Pandey RP, Parajuli P, Koirala N, Park JW, Sohng JK. 2013. Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC. Appl. Environ. Microbiol. 79: 6833-6838. https://doi.org/10.1128/AEM.02057-13
  16. Pandey RP, Parajuli P, Shin JY, Lee J, Lee S, Hong YS, et al. 2014. Enzymatic biosynthesis of novel resveratrol glucoside and glycoside derivatives. Appl. Environ. Microbiol. 80: 7235-7243. https://doi.org/10.1128/AEM.02076-14
  17. Gantt RW, Peltier-Pain P, Thorson JS. 2011. Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules. Nat. Prod. Rep. 28: 1811-1853. https://doi.org/10.1039/c1np00045d
  18. Elshahawi SI, Shaaban KA, Kharel MK, Thorson JS. 2015. A comprehensive review of glycosylated bacterial natural products. Chem. Soc. Rev. 44: 7591-7697. https://doi.org/10.1039/C4CS00426D
  19. Zhang J, Singh S, Hughes RR, Zhou M, Sunkara M, Morris AJ, et al. 2014. A simple strategy for glycosyltransferase-catalyzed aminosugar nucleotide synthesis. Chembiochem 15: 647-652. https://doi.org/10.1002/cbic.201300779
  20. Ati J, Lafite P, Daniellou, R. 2017. Enzymatic synthesis of glycosides: from natural O- and N-glycosides to rare C- and S-glycosides. Beilstein J. Org. Chem. 13: 1857-1865. https://doi.org/10.3762/bjoc.13.180
  21. Pandey RP, Bashyal P, Parajuli P, Yamaguchi T, Sohng JK. 2019. Two trifunctional lelior glycosyltransferases as biocatalysts for natural products glycodiversification. Org. Lett. 21: 8058-8064. https://doi.org/10.1021/acs.orglett.9b03040

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