Exploring the Nucleophilic N-and S-glycosylation Capacity of Bacillus licheniformis YjiC Enzyme.

Exploring the Nucleophilic N-and S-glycosylation Capacity of Bacillus licheniformis YjiC Enzyme. J Microbiol Biotechnol. 2020 Mar 20;: Authors: Bashyal P, Thapa SB, Kim TS, Pandey RP, Sohng JK 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 broad substrate spectrum including UDP-α-D-glucose, UDP-N-acetyl glucosamine, UDP-N-acetyl-galactosamine, 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 promiscuous enzyme to conjugate 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. PMID: 32238768 [PubMed - as supplied by publisher]
Source: Journal of Microbiology and Biotechnology - Category: Biotechnology Authors: Tags: J Microbiol Biotechnol Source Type: research