Aminotransferases for aromatic amino acids and aspartate in Bacillus subtilis

摘要: Abstract Two proteins (form A and B 2 ) with aromatic-amino-acid aminotransferase activity were detected in extracts of Bacillus subtilis . histidinol phosphate (protein 1 for the aromatic amino acids was also present. The aspartate ( l -aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) C) displayed similar activity. Each four isolated free from others by successive application DEAE-cellulose column chromatography flat-bed isoelectric focusing at pH range 4–6. From is major form (aromatic-amino-acid:2-oxoglutarate 2.6.1.57) K m values tyrosine phenylalanine this are somewhat lower than minor A. same range, but enzyme 12–20 times higher corresponding two forms amino-transferase. Apparent molecular weights estimated Sephadex gel filtration to be approx. 73000, 64000, 54000 66000 A, , respectively. Form being reported first time communication.