Steady-State Kinetic Characterization of Evolved Biphenyl Dioxygenase, Which Acquired Novel Degradation Ability for Benzene and Toluene
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- SUENAGA Hikaru
- Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST)
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- SATO Mika
- Department of Bioscience and Biotechnology, Kyushu University
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- GOTO Masatoshi
- Department of Bioscience and Biotechnology, Kyushu University
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- TAKESHITA Mariko
- Department of Bioscience and Biotechnology, Kyushu University Seika Women’s Junior College
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- FURUKAWA Kensuke
- Department of Bioscience and Biotechnology, Kyushu University
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Biphenyl dioxygenase (Bph Dox) catalyzes initial oxygenation in the bacterial biphenyl degradation pathway. Bph Dox in Pseudomonas pseudoalcaligenes KF707 is a Rieske type three-component enzyme in which a large subunit (encoded by the bphA1 gene) plays an important role in the substrate specificity of Bph Dox. Steady-state kinetic assays using purified enzyme components demonstrated that KF707 Bph Dox had a kcat⁄Km of 33.1×103 (M−1 s−1) for biphenyl. Evolved 1072 Bph Dox generated by the process of DNA shuffling (Suenaga, H. et al., J. Bacteriol., 184, 3682–3688 (2002)) exhibited enhanced degradation activity not only for biphenyl (kcat⁄Km of 62.2×103 [M−1 s−1]) but also for benzene and toluene, compounds that are rarely attacked by KF707 Bph Dox. These results suggest that evolved 1072 Bph Dox acquires higher affinities and catalytic efficiencies for various substrates than the original KF707 enzyme.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (4), 1021-1025, 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
- 1390001206476221056
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- NII論文ID
- 10018532876
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 7899991
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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
- Crossref
- CiNii Articles
- KAKEN
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- 使用不可