Functional expression of l -lysine α-oxidase from Scomber japonicus in Escherichia coli for one-pot synthesis of l -pipecolic acid from dl -lysine
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| 024 | 7 | 0 | |a 10.1007/s00253-014-6308-0 |2 doi |
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| 245 | 0 | 0 | |a Functional expression of l -lysine α-oxidase from Scomber japonicus in Escherichia coli for one-pot synthesis of l -pipecolic acid from dl -lysine |h [Elektronische Daten] |c [Yasushi Tani, Ryoma Miyake, Ryoichi Yukami, Yasumasa Dekishima, Hideyasu China, Shigeki Saito, Hiroshi Kawabata, Hisaaki Mihara] |
| 520 | 3 | |a l-Pipecolic acid is a key component of biologically active molecules and a pharmaceutically important chiral building block. It can be stereoselectively produced from l-lysine by a two-step bioconversion involving l-lysine α-oxidase and ∆1-piperideine-2-carboxylae (Pip2C) reductase. In this study, we focused on an l-lysine α-oxidase from Scomber japonicus that was originally identified as an apoptosis-inducing protein (AIP) and applied the enzyme to one-pot fermentation of l-pipecolic acid in Escherichia coli. A synthetic gene coding for an AIP was expressed in E. coli, and the recombinant enzyme was purified and characterized. The purified enzyme was determined to be a homodimer with a molecular mass of 133.9kDa. The enzyme essentially exhibited the same substrate specificity as the native enzyme. Optimal temperature and pH for the enzymatic reaction were 70 °Cand 7.4, respectively. The enzyme was stable below 60°C and at a pH range of 5.5-7.5 but was markedly inhibited by Co2+. To establish a one-pot fermentation system for the synthesis of optically pure l-pipecolic acid from dl-lysine, an E. coli strain carrying a plasmid encoding AIP, Pip2C reductase from Pseudomonas putida, lysine racemase from P. putida, and glucose dehydrogenase from Bacillus subtilis was constructed. The one-pot process produced 45.1g/L of l-pipecolic acid (87.4% yield from dl-lysine) after a 46-h reaction with high optical purity (>99.9% enantiomeric excess). | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2014 | ||
| 690 | 7 | |a l- Lysine α-oxidase |2 nationallicence | |
| 690 | 7 | |a l- Pipecolic acid |2 nationallicence | |
| 690 | 7 | |a One-pot synthesis |2 nationallicence | |
| 690 | 7 | |a Stereoselective synthesis |2 nationallicence | |
| 690 | 7 | |a ∆1-Piperideine-2-carboxylic acid |2 nationallicence | |
| 700 | 1 | |a Tani |D Yasushi |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | |
| 700 | 1 | |a Miyake |D Ryoma |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | |
| 700 | 1 | |a Yukami |D Ryoichi |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | |
| 700 | 1 | |a Dekishima |D Yasumasa |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | |
| 700 | 1 | |a China |D Hideyasu |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | |
| 700 | 1 | |a Saito |D Shigeki |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | |
| 700 | 1 | |a Kawabata |D Hiroshi |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | |
| 700 | 1 | |a Mihara |D Hisaaki |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/12(2015-06-01), 5045-5054 |x 0175-7598 |q 99:12<5045 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-014-6308-0 |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/s00253-014-6308-0 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tani |D Yasushi |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Miyake |D Ryoma |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Yukami |D Ryoichi |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Dekishima |D Yasumasa |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a China |D Hideyasu |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Saito |D Shigeki |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kawabata |D Hiroshi |u Mitsubishi Chemical Group Science and Technology Research Center, Inc., 227-8502, Yokohama, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mihara |D Hisaaki |u Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 525-8577, Kusatsu, Shiga, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/12(2015-06-01), 5045-5054 |x 0175-7598 |q 99:12<5045 |1 2015 |2 99 |o 253 | ||