title: Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates.
abstract: 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.
authors.affiliation: Centre for Industrial Biotechnology and Biocatalysis Department of Biochemical and Microbial Technology, Ghent University, 9000 Ghent, Belgium. tom.desmet@ugent.be.
authors.forename: Chao
authors.initials: C
authors.lastname: Chen
authors.forename: Jef
authors.initials: J
authors.lastname: Van der Borght
authors.forename: Rob
authors.initials: R
authors.lastname: De Vreese
authors.forename: Matthias
authors.initials: M
authors.lastname: D'hooghe
authors.forename: Wim
authors.initials: W
authors.lastname: Soetaert
authors.forename: Tom
authors.initials: T
authors.lastname: Desmet
mesh_terms: D001665:Binding Sites; D005690:Galactose / Q000378:metabolism*; D005964:Glucosyltransferases / Q000737:chemistry / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation; D013379:Substrate Specificity
chemical_list: D010710:Phosphates; D005964:Glucosyltransferases; C023181:alpha,alpha-trehalose phosphorylase; D005690:Galactose