Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphatesElectronic supplementary information (ESI) available: Methods and supporting data. See DOI: 10.1039/c4cc02202e

A two-step process is reported for the anomeric phosphorylation of galactose, using trehalose phosphorylase as biocatalyst. The monosaccharide enters this process as acceptor but can subsequently be released from the donor side, thanks to the non-reducing nature of the disaccharide intermediate. A k...

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Main Authors Chen, Chao, Van der Borght, Jef, De Vreese, Rob, D'hooghe, Matthias, Soetaert, Wim, Desmet, Tom
Format Journal Article
LanguageEnglish
Published 24.06.2014
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Summary:A two-step process is reported for the anomeric phosphorylation of galactose, using trehalose phosphorylase as biocatalyst. The monosaccharide enters this process as acceptor but can subsequently be released from the donor side, thanks to the non-reducing nature of the disaccharide intermediate. A key development was the creation of an optimized enzyme variant that displays a strict specificity (99%) for β-galactose 1-phosphate as product. A variant of trehalose phosphorylase was created that displays a modified specificity and can be used for the anomeric phosphorylation of galactose in a two-step process.
Bibliography:Electronic supplementary information (ESI) available: Methods and supporting data. See DOI
10.1039/c4cc02202e
ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc02202e