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

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Abstract

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-(CH2)11-OPh as substrates. This reaction gave the desired disaccharide Rhaβ-1,4-Glcα-PP-(CH2)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 271DKD273 motif was critical for the enzymatic activity and most likely the binding site for the required divalent metal cation.

Graphical abstract: Biochemical studies of a β-1,4-rhamnoslytransferase from Streptococcus pneumonia serotype 23F

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Publication details

The article was received on 09 Nov 2018, accepted on 07 Jan 2019 and first published on 08 Jan 2019


Article type: Communication
DOI: 10.1039/C8OB02795A
Citation: Org. Biomol. Chem., 2019, Advance Article
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    Biochemical studies of a β-1,4-rhamnoslytransferase from Streptococcus pneumonia serotype 23F

    H. Wang, S. Li, C. Xiong, G. Jin, Z. Chen, G. Gu and Z. Guo, Org. Biomol. Chem., 2019, Advance Article , DOI: 10.1039/C8OB02795A

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