2017 Fiscal Year Final Research Report
Reaction mechanism of novel tryptophan-hydroxylating enzyme involving in quinone cofactor biogenesis
| Project/Area Number |
15K07391
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Applied biochemistry
|
|---|
| Research Institution | Osaka University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
中井 忠志 広島工業大学, 生命学部, 准教授 (00333344)
|
|---|
| Project Period (FY) |
2015-04-01 – 2018-03-31
|
| Keywords | キノン補酵素 / FAD / オキシゲナーゼ |
|---|
| Outline of Final Research Achievements |
We have studied the reaction mechanism and X-ray crystal structure of FAD-dependent monooxygenase QhpG that is involved in the cofactor biogenesis of bactral quinohemoprotein amine dehydrogenase. Our final aim is application of QhpG for a novel tool for peptide engineering. In vitro reaction system for QhpG provided the important information for the chemical structure of the QhpG reaction product. On the basis of X-ray crystal structure of QhpG, we have elucidated the QhpG reaction mechanism including the recognition of the specific Trp residue on the substrate peptide.
|
| Free Research Field |
酵素反応科学、構造生物学
|
