Dye-linked d -amino acid dehydrogenase from the thermophilic bacterium Rhodothermus marinus JCM9785: characteristics and role in trans -4-hydroxy- l -proline catabolism
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| 024 | 7 | 0 | |a 10.1007/s00253-014-6263-9 |2 doi |
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| 245 | 0 | 0 | |a Dye-linked d -amino acid dehydrogenase from the thermophilic bacterium Rhodothermus marinus JCM9785: characteristics and role in trans -4-hydroxy- l -proline catabolism |h [Elektronische Daten] |c [Takenori Satomura, Masaru Ishikura, Takashi Koyanagi, Haruhiko Sakuraba, Toshihisa Ohshima, Shin-ichiro Suye] |
| 520 | 3 | |a A gene from the thermophilic Gram-negative bacterium Rhodothermus marinus JCM9785, encoding a dye-linked d-amino acid dehydrogenase homologue, was overexpressed in Escherichia coli, and its product was purified and characterized. The expressed enzyme was a highly thermostable dye-linked d-amino acid dehydrogenase that retained more than 80% of its activity after incubation for 10min at up to 70°C. When enzyme-catalyzed dehydrogenation of several d-amino acids was carried out using 2,6-dichloroindophenol as the electron acceptor, d-phenylalanine was the most preferable substrate among the d-amino acids tested. Immediately upstream of the dye-linked d-amino acid dehydrogenase gene (dadh) was a gene encoding a 4-hydroxyproline 2-epimerase homologue (hypE). That gene was successfully expressed in E. coli, and the gene product exhibited strong 4-hydroxyproline 2-epimerase activity. Reverse transcription PCR and quantitative real-time PCR showed that the six genes containing the dadh and hypE genes were arranged in an operon and were required for catabolism of trans-4-hydroxy-l-proline in R. marinus. This is the first description of a dye-linked d-amino acid dehydrogenase (Dye-DADH) with broad substrate specificity involved in trans-4-hydroxy-l-proline catabolism. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2014 | ||
| 690 | 7 | |a trans -4-hydroxy- l -proline catabolism |2 nationallicence | |
| 690 | 7 | |a d -amino acid dehydrogenase |2 nationallicence | |
| 690 | 7 | |a Dye-linked dehydrogenase |2 nationallicence | |
| 690 | 7 | |a Thermophilic bacteria |2 nationallicence | |
| 690 | 7 | |a Rhodothermus marinus |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 Ishikura |D Masaru |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 Koyanagi |D Takashi |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, Miki-cho, 761-0795, Kita-gun, Kagawa, 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 | |
| 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 | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/10(2015-05-01), 4265-4275 |x 0175-7598 |q 99:10<4265 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-014-6263-9 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-014-6263-9 |q text/html |z Onlinezugriff via DOI | ||
| 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 Ishikura |D Masaru |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 Koyanagi |D Takashi |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, Miki-cho, 761-0795, Kita-gun, Kagawa, 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 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 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/10(2015-05-01), 4265-4275 |x 0175-7598 |q 99:10<4265 |1 2015 |2 99 |o 253 | ||