Abstract
D-Amino acid aminotransferase and branched-chain L-amino acid aminotransferase show a significant homology in amino acid sequence each other, but little similarity to all other aminotransferases. They are also unique in the stereospecificity for hydrogen transfer at the C-4′ of external Schiff base intermediates: show the pro-R specificity in contrast to other various aminotransferases catalyzing the pro-S hydrogen transfer. This suggests that their topographical situations of the external Schiff base and the catalytic base in the activesite are similar to each other, but different from those of other aminotransferases. X-Ray chrystallographic data of D-amino acid aminotransferase support this hypothesis: The structure of D-amino acid aminotransferase is different from those of other aminotransferases so far studied. Based on the structure, and stereospecificity for C-4′ hydrogen transfer, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase probably evolved from the common ancestral protein, which was different from that of other aminotransferases.
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