Regioselective Phosphorylation of Carbohydrates and Various Alcohols by Bacterial Acid Phosphatases; Probing the Substrate Specificity of the Enzyme from Shigella flexneri

Abstract

Abstract 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.

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Identifiers

DOI

10.1002/adsc.200505072

Journal

Advanced Synthesis & Catalysis

Year

2005