研究者情報 | 神奈川大学

イブカ　アキコ Ibuka Akiko 井深　章子所属神奈川大学化学生命学部生命機能学科神奈川大学大学院理学研究科理学専攻（生物科学領域）職種教授
言語種別	英語
発行・発表の年月	2007/04
形態種別	学術雑誌
査読	査読あり
標題	Val326 of Thermoactinomyces vulgaris R-47 amylase II modulates the preference for alpha-(1,4)- and alpha-(1,6)-glycosidic linkages
執筆形態	共著
掲載誌名	BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
掲載区分	国外
出版社・発行元	ELSEVIER SCIENCE BV
巻・号・頁	1774(4),pp.443-449
著者・共著者	Keisuke Ito,Sohei Ito,Kousuke Ishino,Akiko Shimizu-Ibuka,Hiroshi Sakai
概要	Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) catalyzes not only the hydrolysis of alpha-(1,4)- and alpha-(1,6)-glycosidic linkages but also transglycosylation. We focused on the amino acid residue at the 326th position based on information on the primary structure and crystal structure, and replaced Val with Ala, Ile, or Thr. The V326A mutant favored hydrolysis of the alpha-(1,4)-glycosidic linkage compared to the wildtype enzyme. In contrast, the V3261 mutant favored hydrolysis of the alpha-(1,6)-glycosidic linkage and exhibited low transglycosylation activity. In the case of the V326T mutant, the hydrolytic activity was almost identical to that of the wild-type TVA 11, and the transglycosylation activity was poor. These results suggest that the volume and the hydrophobicity of the amino acid residue at the 326th position modulate both the preference for glycosidic linkages and the transglycosylation activity.
DOI	10.1016/j.bbapap.2007.02.006
ISSN	15709639