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A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer
Y Watanabe1, T Muro, A Sugihara
1Osaka Municipal Technical Research Institute, Japan.
Biochimica Et Biophysica Acta
|January 4, 1997
Abstract:
A newly isolated actinomycete belonging to Saccharothrix sp. was found to produce a unique enzyme catalyzing D-amino acid transfer. The enzyme, which was tentatively named D-amino acid transferase, was purified 2600-fold to electrophoretic homogeneity and the molecular mass was 41 kDa. The enzyme was D-configuration specific and recognized aromatic D-amino acid esters to form oligo D-amino acid esters. D-Phenylalanine ester was favored as substrate over other D-amino acid esters. The optimum conditions for oligo D-phenylalanine ester formation by D-amino acid transferase were pH 7.0 and 40 degrees C. The enzyme was inhibited by DAN, EPNP and DFP.