Dye-linked D-amino acid dehydrogenases: biochemical characteristics and applications in biotechnology

Verfasser / Beitragende:
[Takenori Satomura, Haruhiko Sakuraba, Shin-ichiro Suye, Toshihisa Ohshima]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/22(2015-11-01), 9337-9347
Format:
Artikel (online)
ID: 605500800
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024 7 0 |a 10.1007/s00253-015-6944-z  |2 doi 
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245 0 0 |a Dye-linked D-amino acid dehydrogenases: biochemical characteristics and applications in biotechnology  |h [Elektronische Daten]  |c [Takenori Satomura, Haruhiko Sakuraba, Shin-ichiro Suye, Toshihisa Ohshima] 
520 3 |a 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. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Dye-linked dehydrogenase  |2 nationallicence 
690 7 |a D-Amino acid dehydrogenase  |2 nationallicence 
690 7 |a Flavoenzyme  |2 nationallicence 
690 7 |a Amino acid catabolism  |2 nationallicence 
690 7 |a Electrochemical biosensor  |2 nationallicence 
700 1 |a Satomura  |D Takenori  |u Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan  |4 aut 
700 1 |a Sakuraba  |D Haruhiko  |u Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, 761-0795, Miki-cho, Kita-gun, Kagawa, Japan  |4 aut 
700 1 |a Suye  |D Shin-ichiro  |u Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan  |4 aut 
700 1 |a Ohshima  |D Toshihisa  |u Department of Biomedical engineering, Faculty of Engineering, Osaka Institute of Technology, Ohmiya, 5-16-1 Asahi-ku, 535-8585, Ohsaka, Japan  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9337-9347  |x 0175-7598  |q 99:22<9337  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6944-z  |q text/html  |z Onlinezugriff via DOI 
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908 |D 1  |a review-article  |2 jats 
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950 |B NATIONALLICENCE  |P 700  |E 1-  |a Satomura  |D Takenori  |u Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Sakuraba  |D Haruhiko  |u Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, 761-0795, Miki-cho, Kita-gun, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Suye  |D Shin-ichiro  |u Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, 910-8507, Fukui, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ohshima  |D Toshihisa  |u Department of Biomedical engineering, Faculty of Engineering, Osaka Institute of Technology, Ohmiya, 5-16-1 Asahi-ku, 535-8585, Ohsaka, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9337-9347  |x 0175-7598  |q 99:22<9337  |1 2015  |2 99  |o 253