| Project/Area Number |
26560435
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Biomolecular chemistry
|
|---|
| Research Institution | University of Toyama |
|---|
Principal Investigator |
MORITA HIROYUKI 富山大学, 和漢医薬学総合研究所, 教授 (20416663)
|
|---|
| Project Period (FY) |
2014-04-01 – 2016-03-31
|
| Project Status |
Completed (Fiscal Year 2015)
|
| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
|
|---|
| Keywords | 酵素工学 / ポリケタイド合成酵素 / X線結晶構造解析 / 立体構造解析 |
|---|
| Outline of Final Research Achievements |
In order to modify the function of type III polyketide synthase, we carried out deletion mutagenesis studies on octaketide synthase (OKS), which catalyzes sequential condensations of eight molecules of malonyl-CoA to produce SEK4/SEK4b. The deletion mutagenesis studies revealed that the loss of Varine351, lining the active site cavity of OKS, results in specializing its starter substrate specificity in fatty acyl CoAs. Furthermore, a crystal structure analysis of the mutant enzyme suggested that an expansion of the active-site cavity near catalytic residue, cysteine, specialized the substrate specificity of the mutant in the fatty acyl CoAs.
|
