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Regioselective Phosphorylation of Carbohydrates and Various Alcohols by Bacterial Acid Phosphatases; Probing the Substrate Specificity of the Enzyme from Shigella flexneri
Author(s) -
van Herk Teunie,
Hartog Aloysius F.,
van der Burg Alida M.,
Wever Ron
Publication year - 2005
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200505072
Subject(s) - chemistry , enzyme , phosphorylation , dephosphorylation , shigella flexneri , phosphatase , biochemistry , substrate (aquarium) , escherichia coli , biology , ecology , gene
Bacterial non‐specific acid phosphatases normally catalyze the dephosphorylation of a variety of substrates. As shown previously the enzymes from Shigella flexneri and Salmonella enterica are also able to catalyze the phosphorylation of inosine to inosine monophosphate and D ‐glucose to D ‐glucose 6‐phosphate (D‐G6P) using cheap pyrophosphate as the phosphate donor. After optimization high yields (95%) are achieved in the latter reaction and we show here that it is possible to use these enzymes in a preparative manner. This prompted us to investigate by using 31 P NMR and HPLC also the phosphorylation of a broad range of carbohydrates and alcohols. Many cyclic carbohydrates are phosphorylated in a regioselective manner. Non‐cyclic carbohydrates are phosphorylated as well. Phosphorylation of linear alcohols, cyclic and aromatic alcohols is also possible. In all cases the acid phosphatase from Shigella prefers a primary alcohol function above a secondary one. We conclude that these enzymes are an attractive alternative to existing chemical and enzymatic methods in the phosphorylation of a broad range of compounds.