Characterization of novel quinone containing amino acid oxidases from marine bacterium

2019 Fiscal Year Final Research Report

• Project/Area Number: 17K06926
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biofunction/Bioprocess
• Research Institution: Okayama University
• Principal Investigator: INAGAKI Kenji 岡山大学, 環境生命科学研究科, 教授 (80184711)
• Co-Investigator(Kenkyū-buntansha): 今田 勝巳 大阪大学, 理学研究科, 教授 (40346143)
• Project Period (FY): 2017-04-01 – 2020-03-31
• Keywords: 海洋細菌 / Marinomonas mediterranea / グリシンオキシダーゼ / L-リシン ε-オキシダーゼ / バイオセンサー / システイントリプトフィルキノン / 基質特異性

Outline of Final Research Achievements

The marine bacterium Marinomonas mediterranea produces L-lysine-ε-oxidase (ε-LysOX) and glycine oxidase (GlyOX), both enzymes are involved in extracellular biofilm formation. ε-LysOX contains a built-in coenzyme, cysteine tryptophyllquinone (CTQ), and is an enzyme with strict substrate specificity. In this study, we succeeded in constructing an E. coli expression system for both enzymes in order to analyze the structures and functions of these enzymes and applied development, and were able to establish a purification system. Furthermore, we clarified that both enzymes have strict substrate specificity and are useful for biosensors, and succeeded in establishing the foundation for industrial application.

Free Research Field

生物機能工学

Academic Significance and Societal Importance of the Research Achievements

L-リシン-ε-オキシダーゼ(ε-LysOX)は補酵素としてビルトイン型補酵素のシステイントリプトフィルキノン(CTQ)を持つことがアミノ酸オキシダーゼではじめて判明した酵素であり，グリシンオキシダーゼ(GlyOX)も同様にCTQ依存性で，酵素進化的にも極めて興味深い酵素群である。両酵素ともに極めて基質特異性が厳格な酵素で，バイオセンサーを始め，臨床医薬にも貢献が期待される。今本研究の成果により学術的にも産業的にも利用の進展が期待できる。