A UNIQUE ENZYME FROM SACCHAROTHRIX SP CATALYZING D-AMINO-ACID TRANSFER

Authors
WATANABE Y MURO T SUGIHARA A SHIMADA Y NAGAO T TAKENISHI S TOMINAGA Y
Citation
Y. Watanabe et al., A UNIQUE ENZYME FROM SACCHAROTHRIX SP CATALYZING D-AMINO-ACID TRANSFER, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1337(1), 1997, pp. 40-46
Citations number
29
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1337
Issue
1
Year of publication
1997
Pages
40 - 46
Database
ISI
SICI code
0167-4838(1997)1337:1<40:AUEFSS>2.0.ZU;2-N
Abstract
A newly isolated actinomycete belonging to Saccharothrix sp. was found to produce a unique enzyme catalyzing D-amino acid transfer. The enzy me, which was tentatively named D-amino acid transferase, was purified 2600-fold to electrophoretic homogeneity and the molecular mass was 4 1 kDa. The enzyme was D-configuration specific and recognized aromatic D-amino acid esters to form oligo D-amino acid esters. D-Phenylalanin e ester was favored as substrate over other D-amino acid esters. The o ptimum conditions for oligo D-phenylalanine ester formation by D-amino acid transferase were PH 7.0 and 40 degrees C. The enzyme was inhibit ed by DAN, EPNP and DFP.