Biochemical studies of a β-1,4-rhamnoslytransferase from serotype 23F

A new β-rhamnoslytransferase Cps23FT from Streptococcus pneumonia serotype 23F was expressed and characterized. Its enzymatic activity and function were confirmed for the first time by utilizing enzymatically prepared dTDP-Rha and chemically synthesized Glcα-PP-(CH 2 ) 11 -OPh as substrates. This re...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2019-01, Vol.17 (5), p.171-175
Main Authors: Wang, Hong, Li, Siqiang, Xiong, Chenghe, Jin, Guoxia, Chen, Zonggang, Gu, Guofeng, Guo, Zhongwu
Format: Article
Language:English
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Summary:A new β-rhamnoslytransferase Cps23FT from Streptococcus pneumonia serotype 23F was expressed and characterized. Its enzymatic activity and function were confirmed for the first time by utilizing enzymatically prepared dTDP-Rha and chemically synthesized Glcα-PP-(CH 2 ) 11 -OPh as substrates. This reaction gave the desired disaccharide Rhaβ-1,4-Glcα-PP-(CH 2 ) 11 -OPh in a good isolated yield (67%), suggesting the potential of Cps23FT as a tool enzyme for the synthesis of complex oligosaccharides containing difficult β-rhamnosyl linkages. Furthermore, site-directed mutagenesis of Cps23FT disclosed that its 271 DKD 273 motif was critical for the enzymatic activity and most likely the binding site for the required divalent metal cation. A new β-rhamnoslytransferase Cps23FT from Streptococcus pneumonia serotype 23F was functionally explored for the first time.
ISSN:1477-0520
1477-0539
DOI:10.1039/c8ob02795a