caa a22 4500 605500800 CHVBK 20210128100557.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00253-015-6944-z doi (NATIONALLICENCE)springer-10.1007/s00253-015-6944-z Dye-linked D-amino acid dehydrogenases: biochemical characteristics and applications in biotechnology [Elektronische Daten] [Takenori Satomura, Haruhiko Sakuraba, Shin-ichiro Suye, Toshihisa Ohshima] Dye-linked D-amino acid dehydrogenases (Dye-DADHs) catalyze the dehydrogenation of free D-amino acids in the presence of an artificial electron acceptor. Although Dye-DADHs functioning in catabolism of L-alanine and as primary enzymes in electron transport chains are widely distributed in mesophilic Gram-negative bacteria, biochemical and biotechnological information on these enzymes remains scanty. This is in large part due to their instability after isolation. On the other hand, in the last decade, several novel types of Dye-DADH have been found in thermophilic bacteria and hyperthermophilic archaea, where they contribute not only to L-alanine catabolism but also to the catabolism of other amino acids, including D-arginine and L-hydroxyproline. In this minireview, we summarize recent developments in our understanding of the biochemical characteristics of Dye-DADHs and their specific application to electrochemical biosensors. Springer-Verlag Berlin Heidelberg, 2015 Dye-linked dehydrogenase nationallicence D-Amino acid dehydrogenase nationallicence Flavoenzyme nationallicence Amino acid catabolism nationallicence Electrochemical biosensor nationallicence Satomura Takenori Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan aut Sakuraba Haruhiko Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, 761-0795, Miki-cho, Kita-gun, Kagawa, Japan aut Suye Shin-ichiro Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan aut Ohshima Toshihisa Department of Biomedical engineering, Faculty of Engineering, Osaka Institute of Technology, Ohmiya, 5-16-1 Asahi-ku, 535-8585, Ohsaka, Japan aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/22(2015-11-01), 9337-9347 0175-7598 99:22<9337 2015 99 253 https://doi.org/10.1007/s00253-015-6944-z text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6944-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Satomura Takenori Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan aut NATIONALLICENCE 700 1- Sakuraba Haruhiko Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, 761-0795, Miki-cho, Kita-gun, Kagawa, Japan aut NATIONALLICENCE 700 1- Suye Shin-ichiro Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan aut NATIONALLICENCE 700 1- Ohshima Toshihisa Department of Biomedical engineering, Faculty of Engineering, Osaka Institute of Technology, Ohmiya, 5-16-1 Asahi-ku, 535-8585, Ohsaka, Japan aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/22(2015-11-01), 9337-9347 0175-7598 99:22<9337 2015 99 253