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Biochemistry and biotechnology of amino acid dehydrogenases

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Bioprocesses and Applied Enzymology

Part of the book series: Advances in Biochemical Engineering/Biotechnology ((ABE,volume 42))

Abstract

Over the last decade, amino acid dehydrogenases such as alanine dehydrogenase (Ala DH), leucine dehydrogenase (Leu DH), and phenylalanine dehydrogenase (Phe DH) have been applied to the enantiomer-specific synthesis and analysis of various amino acids. In perticular, amino acid dehydrogenases from thermophiles have received much attention because of their high stability. Their productivity was enhanced and the purification facilitated by the gene cloning. The advances in biotechnological applications of these enzymes are based on fundamental studies concerning characteristics of the enzymes and reaction mechanism as described in this chapter. Further elucidation of the structure and function of these enzymes based on genetic engineering and protein engineering may enable their properties to be improved for their future uses in biotechnology.

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Authors and Affiliations

  1. Department of Chemistry, Kyoto University of Education, Fushimi-ku, 612, Kyoto, Japan

    Toshihisa Ohshima

  2. Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, 611, Kyoto-Fu, Japan

    Kenji Soda

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  1. Toshihisa Ohshima
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  2. Kenji Soda
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© 1990 Springer-Verlag

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Ohshima, T., Soda, K. (1990). Biochemistry and biotechnology of amino acid dehydrogenases. In: Bioprocesses and Applied Enzymology. Advances in Biochemical Engineering/Biotechnology, vol 42. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0000734

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