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 Biosynthesis of Alkaloids. XXVIII. L-Phenylalanine:2-0xoglutarate Aminotransferase from Lobelia inflata L. Plants

H. Šmogrovičová, A. Jindra, and P. Kovács

Department of Biochemistry and Microbiology, Faculty of Pharmacy, Komenský University, Bratislava 1


Abstract: From exts. of the aerial parts of Lobelia inflata, a 100-fold purified prepn. of phenylalanine:2-oxoglutarate aminotransferase was obtained by salting ot with (NH4)2SO4 and chromatog. on Sephadex G-75 and G-200. The optimal activity was in the pH range of 8.0-9.0. The apparent Michaelis const. for phenylalanine was 5.3 × 10-2M and for 2-oxoglutarate 4.6 × 10-5M. The enzyme catalyzed the transamination of other aromatic and aliphatic amino acids in the presence of 2-oxoglutarate as amino group acceptors; aspartic acid and arginine were the most active as donors.

Full paper in Portable Document Format: 264a360.pdf


Chemical Papers 26 (4) 360–366 (1972)

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