Monooxygenation of Nonnative Substrates Catalyzed by Bacterial Cytochrome P450s Facilitated by Decoy Molecules

• Shoji Osami

  Department of Chemistry, Graduate School of Science, Nagoya University Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency

• Watanabe Yoshihito

  Research Center for Materials Science, Nagoya University

抄録

Cytochrome P450s are a family of heme-containing enzymes that catalyze monooxygenation of inert substrates. Bacterial cytochrome P450s are great candidates as biocatalysts for synthetic applications because of their high hydroxylation activity and their high solubility in water. However, the substrate specificity of bacterial cytochrome P450s is generally high, and their low catalytic activities toward nonnative substrates tends to restrict their application as biocatalysts. We have developed a reaction system that utilizes dummy substrates with structures similar to those of natural substrates, as “decoy molecules”. The decoy molecules induce substrate misrecognition of bacterial P450s, leading to the generation of the active species and ultimately enabling them to catalyze the oxidation of nonnative substrates. The catalytic activity and the enantioselectivity are dependent on the structure of the decoy molecules, suggesting that the reactions can be controlled by variation in the designed structure of the decoy molecules.

収録刊行物

• Chemistry Letters

  Chemistry Letters 46 (3), 278-288, 2017

  公益社団法人 日本化学会

キーワード

• Biocatalyst
• Cytochrome P450
• Nonnative substrate

詳細情報

• CRID: 1390001204588547200
• NII論文ID: 130005436531
• DOI: 10.1246/cl.160963
• ISSN: 13480715
• ISSN: 03667022
• Web Site: https://www.journal.csj.jp/doi/pdf/10.1246/cl.160963
• 本文言語コード: en
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