Structural and functional analyses of novel NAD(P)-dependent amino acid dehydrogenases from archaea

Abstract

NAD(P)-dependent amino acid dehydrogenases are oxidoreductase catalyzing the reversible oxidation of amino acids to their oxo or aldehyde analogs in the presence of NAD or NADP. The enzymes are useful for enzymatic analyses of amino acids, oxo acids and special enzymes, and for the enantiospecific synthesis of L-amino acids and their analogs. In contrast to abundant information available about glutamate, alanine, leucine and phenylalanine dehydrogenases, information about the structure and function of lysine, aspartate, threonine dehydrogenases has been rather limited so far. We have developed the functional and structural analyses of novel types of NAD(P)-dependent amino acid dehydrogenases from hyperthermophilic archaea. The enzymological and structural characteristics of the NAD(P)-dependent amino acid dehydrogenases from archaeal strains are here described.