96193-69-0Relevant articles and documents
Optimization of the kinetic resolution of the DL-phospho-monoesters of threonine and serine by random mutagenesis of the acid phosphatase from Salmonella enterica
Van Herk, Teunie,Hartog, Aloysius F.,Ruijssenaars, Harald J.,Kerkman, Richard,Schoemaker, Hans E.,Wever, Ron
, p. 1349 - 1352 (2008/09/16)
Acid phosphatases are enzymes with a broad substrate specificity showing hydrolytic activity towards several different organic phosphate monoesters, such as nucleotides and sugar phosphates. The acid phosphatase from Salmonella enterica ser. typhimurium LT2 (PhoN-Se) is able to hydrolyze O-phospho-DL-threonine to yield L-threonine with a very high enantioselectivity (E > 200). When O-phospho-DL-serine was hydrolyzed by PhoN-Se, D-serine was formed, however, the ee values rapidly dropped to 50 %. Random mutagenesis by error-prone PCR was performed on the phosphatase in order to increase its enantioselectivity in the formation of D-serine. Two variants with increased selectivity from a library of 9600 mutants have been found, N151D and V78L showing E values of 18.1 and 4.1, respectively, compared to 3.4 for the wild-type (WT) enzyme.
