A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.
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.
Watanabe
Y
Y
Osaka Municipal Technical Research Institute, Japan.
Muro
T
T
Sugihara
A
A
Shimada
Y
Y
Nagao
T
T
Takenishi
S
S
Tominaga
Y
Y
D000192:Actinomycetales / Q000201:enzymology*; D000217:Acyltransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D019881:Aminoacyltransferases; D001426:Bacterial Proteins; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007536:Isomerism; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; C034515:phenylalanine methyl ester; D010649:Phenylalanine; D000217:Acyltransferases; D019881:Aminoacyltransferases; C103932:D-amino acid transferase, Saccharothrix