Glycosylation of Small Molecule Using Flexible Glycosyltransferase

 

Academic reportGlycosylation of Small Molecule Using Flexible Glycosyltransferase

 

Date2014.2.18/Feb. 18,下午/pm13:30-14:30

Location:  Shuhua Hall, Life Sciences Building

Repter:    Prof. Jae Kyung Sohng

Department of Pharmaceutical Engineering

Sun Moon University, Korea 

 

报告摘要/Abstract

       A UDP-glycosyltransferase, YjiC from Bacillus licheniformis DSM13 was exploited for the glycosylation of a number of small molecules. The in-vitro glycosyltransferase assay using YjiC lead to the production of multiple glucosides of polyhydroxyl groups containing aromatic/phenolic as well as aliphatic small molecules exhibiting wide substrate flexibility of the enzyme. We tested the activity of the enzyme with different classes of flavonoids, isoflavonoids, stilbenes, xanthonoids, curcuminoids, benzoates, salicylic acids, and other available compounds in the laboratory. Moreover, we have found the wide donor substrate flexibility of YjiC with different NDP-sugars (UDP-sugars, TDP-sugars, GDP-sugars) transferring a range of modified sugars including L- and D-sugars to the selected acceptors which guide to the production of a number of novel derivatives of natural products. But, it is found that YjiC could transfer only at limited positions of the polyhydroxylated compounds with diverse NDP-sugar donors. We further successfully applied YjiC for the in-vivo biotransformation of different flavonoids using engineered E. coli in large scale fermentor to produce glucosylated derivatives. In conclusion, it is found that YjiC has wide donor as well as acceptor substrates flexibility with high catalytic activity. The further exploitation of such glycosyltransferases could help to efficient production of glycosylated derivatives of natural products which might have potential therapeutic as well as cosmetic applications. However, it is important to carry out enzyme’s structure elucidation and mutagenesis studies to engineer enzyme to develop YjiC as regiospecific glycosyltransferase for the target compound production.

 

 

Viewed:1568

Copyright © State Key Laboratory of Microbial Metabolism. ALL Rights Reserved