Elucidation of mobile loop functions in food-related enzymes
| Project/Area Number |
24380054
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
MIKAMI Bunzo 京都大学, (連合)農学研究科(研究院), 教授 (40135611)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥16,510,000 (Direct Cost: ¥12,700,000、Indirect Cost: ¥3,810,000)
Fiscal Year 2014: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2013: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2012: ¥8,710,000 (Direct Cost: ¥6,700,000、Indirect Cost: ¥2,010,000)
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| Keywords | 応用構造生物学 / タンパク質工学 / 酵素工学 / X線結晶構造解析 / 酵素反応機構 / タンパク質結晶構造解析 / 構造生物学 / タンパク質構造変化 / 食品関連酵素 / 酵素反応 |
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| Outline of Final Research Achievements |
The functions of proteins are usually expressed by conformational changes in loop regions. We have investigated the mobile loops in food-related enzymes that are used in food industry. The mobile loops in the active sites of beta-amylase and alginate lyase that are important for incorporation of substrate and release of product are analyzed by X-ray crystal analyses of their mutant enzymes. The x-ray analysis of the mutants of pro protein-glutaminase (A47Q, A47E) showed that this enzyme can catalyze the reverse reaction in its catalytic pocket. The 24mer peptide derived from pro-region of transglutaminase inhibited the enzyme. We have determined the structure of the enzyme/peptide complex by x-ray analysis.
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Report
(4 results)
Research Products
(32 results)
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[Journal Article] Preliminary X-ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein.2015
Author(s)
Maruyama, N., Goshi, T., Sugiyama, S., Niiyama, M., Adachi, H., Takano, K., Murakami, S., Inoue, T., Mori, Y., Matsumura, H., Mikami, B.
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Journal Title
Acta Crystallogr. F Struct. Biol. Commun.
Volume: 71
Issue: 2
Pages: 132-135
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD⁺-dependent dismutase from Mesorhizobium loti.2015
Author(s)
Mugo, A.N,. Kobayashi, J., Mikami, B., Yoshikane, Y., Yagi, T., Ohnishi, K.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 456
Issue: 1
Pages: 35-40
DOI
Related Report
Peer Reviewed / Open Access
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