title: A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.
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.
authors.affiliation: Osaka Municipal Technical Research Institute, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Watanabe
authors.forename: T
authors.initials: T
authors.lastname: Muro
authors.forename: A
authors.initials: A
authors.lastname: Sugihara
authors.forename: Y
authors.initials: Y
authors.lastname: Shimada
authors.forename: T
authors.initials: T
authors.lastname: Nagao
authors.forename: S
authors.initials: S
authors.lastname: Takenishi
authors.forename: Y
authors.initials: Y
authors.lastname: Tominaga
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; C034515:phenylalanine methyl ester; D010649:Phenylalanine; D000217:Acyltransferases; D019881:Aminoacyltransferases; C103932:D-amino acid transferase, Saccharothrix