2017 Fiscal Year Final Research Report
Critical essence hidden in two catabolic enzymes for biological pigments
| Project/Area Number |
15K05555
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bio-related chemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Keywords | ヘム代謝 / 反応機構 / 結核菌 / 黄色ブドウ球菌 / 酸素添加 |
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| Outline of Final Research Achievements |
In this study, we have elucidated unique reaction mechanisms of new-type heme-degrading enzymes, MhuD from Mycobacterium tuberculosis and IsdG from Staphylococcus aureus, both of which bind heme in highly distorted conformation. MhuD successively catalyzes mono- and di-oxygenation reactions in a single active site. This is the first discovery of the enzyme that fuses the two distinct reactions, leading to the produce the unique heme catabolites of MhuD. Reaction analysis on IsdG reveals, contrary to previous reports, that the MhuD-type reaction becomes dominant under normal reaction conditions. The HCHO release reported is enhanced by increasing reduction rates. This mechanism may be biologically relevant to regulate the HCHO biosynthesis in S. aureus. Furthermore, fluorogenic proteins that bind new heme catabolites as pigments have been developed mainly for their detection with high sensitivity.
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| Free Research Field |
生物無機化学
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