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<B>Establishment of enzymatic reaction system of bacteriochlorophyll <I>c</I> C-20 methyltransferase BchU in a green sulfur bacterium <I>Chlorobium tepidum</I></B>
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- Yaeda Yuki
- Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan Univ.
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- Harada Jiro
- Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan Univ.
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- Saga Yoshitaka
- Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan Univ.
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- Oh-oka Hirozo
- Department of Biology, Graduate School of Science, Osaka Univ.
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- Tamiaki Hitoshi
- Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan Univ.
Bibliographic Information
- Other Title
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- <B>緑色硫黄光合成細菌<I>Chlorobium tepidum</I>におけるバクテリオクロロフィル<I>c</I>のC-20位のメチル化酵素BchUの酵素反応系の確立</B>
Description
The main parts of chlorosomes in green sulfur bacteria are self-aggregates of BChls-c/d/e without support of proteins. We have reported that novel compounds prepared by organic synthetic methods self-aggregated under various conditions in vitro to form similar oligomers with natural chlorosomes. Such organic synthetic procedures are limited because introduction of a methyl group to a specific site in a tetrapyrrole ring is difficult to be carried out. As chlorosomal BChls have many methyl groups, efficient methylation is necessary to prepare various model compounds containing methyl groups specifically. Recently, BChl c biosynthetic pathway in Chlorobium tepidum has been postulated. We focused on the methyltransferases in the pathway, and attempted to utilize these enzymes for introducing methyl groups in vitro. In this study, we cloned BChl c 20-methyltranferase gene, bchU, and overexpressed it in E. coli. We are now going to measure BchU enzymatic activity with many substrates.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2004 (0), 674-674, 2004
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390001205627832832
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- NII Article ID
- 130006988124
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed
