Mutational analyses for product specificity of YjiC towards α-mangostin mono-glucoside

Enzyme and Microbial Technology
Tae-Su KimJae Kyung Sohng

Abstract

Glycosyltransferases (GTs) are key enzymes for the post-modification of secondary metabolites in drug development processes. In our prior research, an one-pot enzymatic system produced α-mangostin 3,6-di-O-β-D-glucopyranoside (Mg1) at a higher proportion using wild-type glycosyltransferase (YjiC) but α-mangostin 3-O-β-D-glucopyranoside (Mg2) exhibited markedly higher anti-bacterial activities. This study focuses on a Bacillus licheniformis-originated flexible glycosyltransferase by mutagenesis to examine the active site residues involved in glycosylation for a product specificity towards Mg2. The generated H298A, H298S, and H298C mutants of YjiC exhibited a regiospecificity towards glycosylated product (Mg2) and were targeted in this study. The production pattern of Mg1 decreased to 63 (H298A), 85 (H298S) and 95% (H298C) yields compared to the wild-type YjiC. The increase of uridine 5'-diphosphate (UDP) leading to the inhibition of enzyme activity and production of uridine 5'-diphosphate glucose (UDP-glucose) in overall system was critical for the specific glycosylated product formation rate. H298A, H298S, and H298C mutants and YjiC exhibited 244, 251, and 186% increases in Mg2 production yields, respectively. And also H298A, H...Continue Reading

Citations

Oct 18, 2019·Chembiochem : a European Journal of Chemical Biology·Ryan R HughesJon S Thorson
Nov 6, 2020·International Journal of Biological Macromolecules·Bing LiuRui Bao
Jun 12, 2020·Biochemistry·Rakesh MaharjanShin-Ichi Ozaki

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