Catalytic Properties of Domain-Exchanged Chimeric Proteins between Firefly Luciferase and<i>Drosophila</i>Fatty Acyl-CoA Synthetase CG6178
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- OBA Yuichi
- Graduate School of Bioagricultural Sciences, Nagoya University
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- TANAKA Kiichi
- Graduate School of Bioagricultural Sciences, Nagoya University
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- INOUYE Satoshi
- Yokohama Research Center, Chisso Co.
書誌事項
- タイトル別名
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- Catalytic Properties of Domain-Exchanged Chimeric Proteins between Firefly Luciferase and Drosophila Fatty Acyl-CoA Synthetase CG6178
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Firefly luciferase and fatty acyl-CoA synthetase are members of the acyl-CoA synthetase super family, which consists of a large N-terminal domain and a small C-terminal domain. Previously we found that firefly luciferase has fatty acyl-CoA synthetic activity, and also identified that the homolog of firefly luciferase in Drosophila melanogaster (CG6178) is a fatty acyl-CoA synthetase and is not a luciferase. In this study, we constructed chimeric proteins by exchanging the domain between Photinus pyralis luciferase (PpLase) and Drosophila CG6178, and determined luminescence and fatty acyl-CoA synthetic activities. A chimeric protein with the N-terminal domain of PpLase and the C-terminal domain of CG6178 (Pp/Dm) had luminescence activity, showing approximately 4% of the activity of wild-type luciferase. The Pp/Dm protein also had fatty acyl-CoA synthetic activity and the substrate specificity was similar to PpLase. In contrast, a chimeric protein with the N-terminal domain of CG6178 and the C-terminal of PpLase (Dm/Pp) had only fatty acyl-CoA synthetase activity, and the substrate specificity was similar to CG6178. These results suggest that the N-terminal domain of firefly luciferase is essential for substrate recognition, and that the C-terminal domain is indispensable but not specialized for the luminescence reaction.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (11), 2739-2744, 2006
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681454257536
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- NII論文ID
- 10018525027
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 8560715
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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