Relationship between 3D-structure and substrate specificity of phospholipase A2 from Echinoderm.
Project/Area Number |
19580230
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Fisheries chemistry
|
Research Institution | Hokkaido University |
Principal Investigator |
KISHIMURA Hideki Hokkaido University, 大学院・水産科学研究院, 准教授 (50204855)
|
Co-Investigator(Kenkyū-buntansha) |
SEKIZAKI Haruo 北海道医療大学, 薬学部, 教授 (50094834)
TOYOTA Eiko 北海道医療大学, 薬学部, 教授 (00103200)
IYAGUCHI Daisuke 北海道医療大学, 薬学部, 講師 (00433425)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | 棘皮動物 / 酵素 / ホスホリパーゼA2 / 基質極性基特異性 / X線結晶構造解析 / 立体構造 / 魚類 / トリプシン / ボスホリパーゼA2 / X線結晶解析 / ヒトデ / リン脂質 |
Research Abstract |
Few researches exist on the relationship between 3D-structure and function of enzyme from marine organisms. In this study, we succeeded the crystallization of anchovy (Engraulis japonica) trypsin and demonstrated its 3D-structure by X-ray crystallography. On the base of this result, we tried to reveal the structural properties of phospholipase A2 from the starfish Patiria pectinifera. The starfish phospholipase A2 is adequate enzyme for production of soybean lysolecithin which is good emulsifier on food industry. Consequently, we determined the full mRNA sequence of the starfish phospholipase A2 and developed the condition for crystallization of the enzyme.
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Report
(4 results)
Research Products
(8 results)