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Amino acid dehydrogenases applications

T. Ohshima and K. Soda, Thermostable amino acid dehydrogenases applications and gene cloning, Trends Biotechnol. 1989a, 7, 210-214. [Pg.206]

In an original application, Yasuda et al have used both l-AAO and d-AAO, and L-lysine oxidase to oxidize o ,Ci -diamino acids. The reactions produce the expected a-keto w-amino acid products, but these then spontaneously cyclize to form cyclic a-imino acids. These compounds are then substrates for the authors recently discovered A methyl amino acid dehydrogenase (NMAADH) from Pseudomonas putida, producing the pure L-cyclic amino acid (Scheme 5). [Pg.75]

Reductive amination reactions of keto acids are performed with amino acid dehydrogenases. NAD-dependent leucine dehydrogenase from Bacillus sp. is of interest for the synthesis of (S)-fert.-leucine [15-17]]. This chiral compound has found widespread application in asymmetric synthesis and as a building block of biologically active substances. The enzyme can also be used for the chemoenzy-matic preparation of (S)-hydroxy-valine [18] and unnatural hydrophobic bran-ched-chain (S)-amino acids. NAD-dependent L-phenylalanine dehydrogenase from Rhodococcus sp. [19] has been used for the synthesis of L-homophenyl-alanine ((S)-2-Amino-4-phenylbutanoic acid) [9]. These processes with water-soluble substrates and products demonstrate that the use of coenzymes must not... [Pg.147]

Ohshima, T., Soda, K. Stereoselective Biocatalysis Amino Acid Dehydrogenases and Their Applications. In Stereoselective Biocatalysis, Patel, R. N. Ed., Marcel Dekker, Inc. New York, 2000, p. 877. [Pg.394]

The coupling of these two enzymatic systems could find many more applications due to the avaUabihty of amino acid dehydrogenases of broader specificity [31]. A series of amino acid dehydrogenases with D-specificity for the preparation of D-amino acids has been applied to the reductive amination of a-keto acids [32]. However, the deracemization of rac-amino acids exploiting this type of enzyme requires an amino acid oxidase with L-specificily, which is a rare enzymatic activity. As an alternative the a-oxo acid, usually available through difficult synthetic procedures, can be used directly. [Pg.204]

Table 13.2 Applications of amino acid dehydrogenase-catalyzed reactions, azide and imine reduction reactions for API synthesis. Table 13.2 Applications of amino acid dehydrogenase-catalyzed reactions, azide and imine reduction reactions for API synthesis.
R.L. Hanson, Preparation of chiral amino acid intermediates for synthesis of pharmaceutical compounds using amino acid dehydrogenases. Asymmetric Synthesis and Application of ( Amino Acids, Chapter 19, pp. 306-321 ACS Symposium Series, vol. 1009. [Pg.405]

T. Ohshima, K. Soda, in R.N. Patel (Ed.), Amino acid dehydrogenases and their applications in Stereoselective Biocatalysis, Marcel and Dekker, New York, 2000, pp. 877-903 page. [Pg.405]

Stereoselective Biocatalysis Amino Acid Dehydrogenases and Their Applications... [Pg.877]

At the beginning of the 1980s, the wide screening of aromatic amino acid dehydrogenases led to the discovery of PheDH in Brevibacterium species [26]. The enzyme was isolated from several mesophiles—Bacillus sphaericus [27], Sporosarcina ureae [27], B. badius [28], Rhodococcus sp. [29], Nocardia sp. [30] and Microbacterium sp. [31], and also from the thermophile T. intermedius [32]—and characterize (Table 5). The enzyme acts on L-norleucine, L-methionine, L-norvaline, and L-tyrosine besides L-phenylalanine in the presence of NAD, although slowly. L-Tryptophan, L-alanine, and D-phenyManine are inert as the substrate. The enzyme shows lower substrate specificity for 2-oxo acids than that for amino acids like AlaDH and LeuDH. The values for ammonia are more than 70 mM. The T. intermedius PheDH is the most thermostable and a useful catalyst for industrial and clinical applications. The enzyme is easily and effectively purified from the recombinant E. coli [6] and commercially available (Unitika Ltd.). [Pg.883]

Extensive research on characteristics and structure of amino acid dehydrogenases reflects their usefulness for application in industry and other fields. In particular, L-amino acids, which are substrates in oxidative deamination and products in reductive amination, are a very important nutrient, and are also starting materials in pharmaceutical compounds. Amino acid dehydrogenases have been used for the stereospecific synthesis of amino acids from achiral substrates, 2-oxo acids, and ammonia, and for analysis of L-amino acids, oxo acids, ammonia, and assay of enzymes of which amino acids and oxo acids are their substrates or products. Some applications of amino acid dehydrogenases are described in this section. [Pg.893]

C. Application of Amino Acid Dehydrogenases to Enzymatic Analysis... [Pg.899]

From the very successful developments of the alcohol dehydrogenase technology for production of secondary alcohols and enzymatic reductive amination of keto-acids for production of amino acids, it is expected that we will also soon see applications for other enzymatic redox chemistries for example, reduction of unsaturated carbonyl compounds with... [Pg.328]

The biochemical characterization of several alcohol dehydrogenases and their exploitation potential demonstrate that these enzymes are most important tools for biochemists. Amino acid sequences of several ADFls are available so far, and alignment studies allow to establish ADH families and to consider their probable evolutionary relationships. For preparative applications, however, particular properties of an enzyme are essential prerequisites, such as enzyme stability and availability, its substrate specificity, or reaction selectivity. Enzymes with NAD as coenzyme are clearly preferred to NADP-dependent ones in practice, because NAD has a significantly higher stability [186-188], a lower price and, is in general, easier to regenerate. [Pg.173]


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See also in sourсe #XX -- [ Pg.893 , Pg.894 , Pg.895 , Pg.896 , Pg.897 , Pg.898 ]




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