Biochimica et Biophysica Acta 1997-01-04

A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.

Y Watanabe, T Muro, A Sugihara, Y Shimada, T Nagao, S Takenishi, Y Tominaga

Index: Biochim. Biophys. Acta 1337(1) , 40-6, (1997)

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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.