- 1) Ohshima, T., and Soda, K., Biochemistry and biotechnology of amino acid dehydrogenases. Adv. Biochem. Eng. Biotechnol., 42, 187–189 (1990).
- 2) Olson, J. A., and Anfinsen, C. B., Kinetic and equilibrium studies on crystalline L-glutamic acid dehydrogenase. J. Biol. Chem., 202, 841–856 (1953).
- 3) Struck, J., and Sizer, I. W., The substrate specificity of glutamate dehydrogenase. Arch. Biochem. Biophys., 86, 260–266 (1960).
- 4) Britton, K. L., Baker, P. J., Engel, P. C., Rice, D. W., and Stillman, T. J., Evolution of substrate diversity in the superfamily of amino acid dehydrogenases: Prospects for rational chiral synthesis. J. Mol. Biol., 234, 938–945 (1993).
- 5) Britton, K. L., Baker, P. J., Rice, D. W., and Stillman, T. J., Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases. Eur. J. Biochem., 209, 851–859 (1992).
- 6) Stillman, T. J., Baker, P. J., Britton, K. L., and Rice, D. W., Conformational flexibility in glutamate dehydrogenase: role of water in substrate recognition and catalysis. J. Mol. Biol., 234, 1131–1139 (1993).
- 7) Baker, P. J., Britton, K. L., Engel, P. C., Farrants, G. W., Lilley, K. S., Rice, D. W., and Stillman, T. J., Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins, 12, 75–86 (1992).
- 8) Khan, M. I. H., Ito, K., Kim, H., Ashida, H., Ishikawa, T., Shibata, H., and Sawa, Y., Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis. Biosci. Biotechnol. Biochem., in press.
- 9) Hashimoto-Gotoh, T., Mizuno, T., Ogasahara, Y., and Nakagawa, M., An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis. Gene, 152, 271–275 (1995).
- 10) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
- 11) Yang, Z., Savchenko, A., Yakunin, A., Zhang, R., Edwards, A., Arrowsmith, C., and Tong, L., Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J. Biol. Chem., 278, 8804–8808 (2003).
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Altering the Substrate Specificity of Glutamate Dehydrogenase from Bacillus subtilis by Site-Directed Mutagenesis
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