Screening of novel inhibitors to hydrogen sulfide-producing enzymes -based on enzyme structures and reaction mechanisms- that can prevent oral malodor
| Project/Area Number |
25462897
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Functional basic dentistry
|
|---|
| Research Institution | Iwate Medical University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Yasuo 愛知学院大学, 歯学部, 准教授 (10315096)
|
|---|
| Project Period (FY) |
2013-04-01 – 2016-03-31
|
| Project Status |
Completed (Fiscal Year 2015)
|
| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
|
|---|
| Keywords | 硫化水素産生酵素 / 酵素 / 歯周病 / 口臭 / 化合物スクリーニング / 反応中間体 / 硫化水素産生 |
|---|
| Outline of Final Research Achievements |
Structral and enzymatic analyses of hydrogen sulfide-producing enzymes from a periodontal pathogen, Fusobacterium nucleatum, were performed. We identified four important amino acid residues on catalysis and/or substrate (reaction intermediate) binding, and revealed their roles and contributions to the catalytic activity. On the basis of these results, the reaction mechanism of hydrogen sulfide-producing enzyme Fn1055 was proposed. In parallel, we constructed two assay systems for inhibitor screening. Using the assay systems, small molecules from chemical libraries were screened.
|
Report
(4 results)
Research Products
(16 results)
-
[Journal Article] Acyl-CoA reductase PGN_0723 utilizes succinyl-CoA to generate succinate semialdehyde in a butyrate-producing pathway of Porphyromonas gingivalis2016
Author(s)
1. Yoshida, Y., Sato, M., Kezuka, Y., Hasegawa, Y., Nagano, K., Takebe, J. and Yoshimura, F.
-
Journal Title
Arch. Biochem. Biophys.
Volume: 596
Pages: 138-148
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
