Abstract
D-Amino acid aminotransferase and branched-chain L-amino acid aminotransferase, which show a significant sequence homology, 6 are unique in their stereospecific catalysis of pro-R C-4'hydrogen transfer through the coenzyme-substrate Schiff base intermediates in contrast to other various aminotransferases catalyzing the pro-S hydrogen transfer. D-Amino acid aminotransfcrase abstracted (R)- 1 H from (4'S)-[4'- 2 H]pyridoxase in a half reaction of transamination with an amino acceptor. Branched-chain L-amino acid aminotransferase catalyzed the pro-R specific hydrogen exchange of pyridoxamine 5'-phosphate with the solvent hydrogen
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