Summary
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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References
Dunathan, H. C. and Voet, J. G. (1974) Stereochemical evidence for the evolution of pyridoxalphosphate enzymes of various function from a common ancestors. Proc.Natl.Acad.Sci. U.S.A. 71, 3888–3891.
Kuramitsu, S., Ogawa, T., Ogawa, H., Kagamiyama, H. (1985) Branched-chain amino acid aminotransferase of Esherichia coli: Nucleotide Sequence of ilvE Gene and the deduced amino acid sequence. J. Biochem. (Tokyo) 97: 993–999.
Metha, P., Hale, T.I., and Christen, P. (1993) Aminotransferases: Demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem 214: 549–561.
Tobler, H.P., Christen, P., Gehring, H. Stereospecifiic labilization of the C-4’ pro-S hydrogen of pyridoxamine 5’-phosphate in aspartate aminotransferase. (1986) J.Biol.Chem, 261: 7105–7108.
Tanizawa, K., Asano, S., Masu, Y., Kuramitsu, S., Kagamiyama, H., Tanaka, H., Soda, K. (1989) The primary structure of Thermostable D-amino acid aminotransferase from a Thermophilic Bacillus spiecies and its correlation with L-amino acid aminotransferase. J. Biol. Chem 264: 2450–2454.
Watanabe, N., Yonaha, K., Sakabe, K., Sakabe, N., Aibara, S., and Morita, Y. (1990) Cryatal structure of co-amino acid: pyruvate aminotransferase. In: Fukui,T., Kagamiyama, H., Soda, K., and Wada, H. (eds.): Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors, Pergamon Press, Oxford, pp. 121–124.
Yoshimura, T., Nishimura, K., Ito, J., Esaki, N., Kagamiyama, H., Manning, J. M., and Soda, K. Unique Stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4’ hydrogen transfer of the coenzyme. J. Am. Chem. Soc 115: 3897–3900.
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Soda, K., Yoshimura, T., Esaki, N. (1994). Stereospecificity of aminotransferases for C-4′ hydrogen transfer and enzyme evolution. In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_3
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DOI: https://doi.org/10.1007/978-3-0348-7393-2_3
Publisher Name: Birkhäuser Basel
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