d -AMINO ACID TRANSAMINATION IN BACILLUS ANTHRACIS

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Abstract
Cell-free extracts of B. anthracis catalyzed a series of transamination reactions involving D-amino acids. In general, the active D-amino acids transaminated with pyruvic acid but not with alpha-ketoglutaric acid, while the corresponding L-isomers were active with alpha-ketoglutaric acid but not with pyruvic acid. Of the amino acids tested the only L-isomer active with pyruvic acid was that of glutamic acid, and the only D-isomer active with alpha-ketoglutaric acid was that of alanine. When extracts were dialyzed, the activity with L-amino acids was reduced or eliminated while most of the activity with D-amino acids was maintained. Extracts contained an active alanine racemase which converted either isomer to a DL-mixture. The most active transamination involving D-amino acids was that between D-phenylalanine and pyruvic acid. A balance of the products and reactants in this reaction was obtained, showing the reaction to be a true transamination reaction.