project started in 1998
Acid phosphatases were originally studied because the binding pocket for vanadate in vanadium CPO was shown by us to be the same as that in a group of acid phosphatases.
Two recombinant acid phosphatases were successfully expressed in E.coli en we have isolated these enzymes in good yield.
We study the phosphorylation of a variety of alcohols and carbohydrates using cheap pyrophosphate. We have also shown that these enzymes are able to phosphorylate dihydroxyacetone to dihydroxyacetone phosphate using pyrophosphate.
Dihydroxyacetone phosphate is a substrate for aldolase and we have developed a one-pot two-enzyme procedure to synthesize a variety of compounds from aldehydes that up to now could only be synthesized via a number of steps.
We have also studied the enantioselective dephosphorylation of racemic DL threonine and DL serine. By a directed evolution approach we have obtained mutants that show an increases enantioselectivity. We expect that these acid phosphatases will be of growing importance for synthetic applications.