Skip to Content
Merck
  • A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.

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

Biochimica et biophysica acta (1997-01-04)
Y Watanabe, T Muro, A Sugihara, Y Shimada, T Nagao, S Takenishi, Y Tominaga
PMID9003435
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.