トップ›研究者を探す›好熱性放線菌が持つシクロデキストリン代謝・膜間輸送マシーナリーの構造学的研究

好熱性放線菌が持つシクロデキストリン代謝・膜間輸送マシーナリーの構造学的研究

KAKEN 科学研究費助成事業データベース で見る
研究課題番号 KAKENHI-PROJECT-16370048
研究種目 基盤研究(B)
研究分野 生物系
生物学
生物科学
構造生物化学
研究機関 香川大学
代表研究者 神鳥 成弘
研究分担者 坂野 好幸
研究分担者 吉田 裕美
研究期間 開始年月日 2004/4/1
研究期間 終了年度 2005
研究ステータス 完了 (2005/4/1)
配分額（合計） 15,000,000 (直接経費 :15,000,000)
配分額（履歴） 2005年度：4,600,000 (直接経費 :4,600,000)
2004年度：10,400,000 (直接経費 :10,400,000)
キーワード X線結晶解析
シクロデキストリン
好熱性放線菌
膜間輸送
オリゴ糖
代謝系
ミュータント酵素
放射光
X-ray structure
cyclodextrin
Thermoactinomyces vulgaris R47
transporter
oligosaccharide
metabolism
mutant enzyme
synchrotron radiation

研究成果

[雑誌論文] Structure of a Complex of Thermoactinomyces vulgaris R-47 α-Amylase 2 with Maltohexaose Demonstrates the Important Role of Aromatic Residues at the Reducing End of the Substrate Binding Cleft.

Ohtaki, A., Mizuno, M., Yoshida, H., Tonozuka, T., Sakano, Y., Kamitori, S. 2006

[雑誌論文] Structure of a Complex of Thermoactinomyces vulgaris R-47 α-Amylase 2 with Maltohexaose Demonstrates the Important Role of Aromatic Residues at the Reducing End of the Substrate Binding Cleft.

Ohtaki, A., Mizuno, M., Yoshida, H., Tonozuka, T., Sakano, Y., Kamitori, S. 2006

[雑誌論文] Structure of a Complex of Thermoactinomyces vulgaris R-47 α-Amylase 2 with Maltohexaose Demonstrates the Important Role of Aromatic Residues at the Reducing End of the Substrate Binding Cleft.

Ohtaki, A., Mizuno, M., Yoshida, H., Tonozuka, T., Sakano, Y., Kamitori, S. 2006

[雑誌論文] Mutagenesis and structural analysis of Thrmoactinomyces vulgaris R-47 α-amylase II (TVA II)

Mizuno, M., Ichikawa, K., Tonozuka, T., Ohtaki, A., Shimura, Y., Kamitori, S., Nishikawa, A., Sakano, Y. 2005

[雑誌論文] Crystallization and preliminary X-ray analysis of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylase

Ichikawa, K., Tonozuka, T., Mizuno, M., Tanabe, Y., Kamitori, S., Nishikawa, A., Sakano, Y. 2005

[雑誌論文] Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1, 6) glycosidic linkages.

Abe, A., Yoshida, H., Tonozuka, T., Sakano, Y., Kamitori, S. 2005

[雑誌論文] Mutagenesis and structural analysis of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII).

Mizuno, M., Ichikawa, K., Tonozuka, T, Ohtaki, A., Shimura, Y., Kamitori, S., Nishikawa, A., Sakano, Y. 2005

[雑誌論文] Mutagenesis and structural analysis of Thermoactinomyces vulgarius R-47 α-amylase II (TVAII).

Mizuno, M., Ichikawa, K., Tonozuka, T., Ohtaki, A., Shimura, Y., Kamitori, S.et al. 2005

[雑誌論文] Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages.

Abe, A., Yoshida, H., Tonozuka, T., Sakano, Y., Kamitori, S. 2005

[雑誌論文] Crystallization and preliminary X-ray analysis of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylase

Ichikawa, K., Tonozuka, T., Mizuno, M., Tanabe, Y., Kamitori, S., Nishikawa, A., Sakano, Y. 2005

[雑誌論文] Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.

Ohtaki, A., Mizuno, M., Tonozuka, T., Sakano, Y., Kamitori, S. 2004

[雑誌論文] Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.

Ohtaki, A., Mizuno, M., Tonozuka, T., Sakano, Y., Kamitori, S. 2004

[雑誌論文] Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.

Ohtaki, A., Mizuno, M., Tonozuka, T., Sakano, Y., Kamitori, S. 2004