1IZK

Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme w398v

1IZK の概要

• エントリーDOI: 10.2210/pdb1izk/pdb
• 関連するPDBエントリー: 1IZJ 1JI1
• 分子名称: amylase, CALCIUM ION (3 entities in total)
• 機能のキーワード: alpha-beta barrele, hydrolase
• 由来する生物種: Thermoactinomyces vulgaris
• 細胞内の位置: Secreted: Q60053
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71143.44

構造登録者

Ohtaki, A.,Iguchi, A.,Mizuno, M.,Tonozuka, T.,Sakano, Y.,Kamitori, S. (登録日: 2002-10-03, 公開日: 2003-07-29, 最終更新日: 2023-12-27)

主引用文献

Ohtaki, A.,Iguchi, A.,Mizuno, M.,Tonozuka, T.,Sakano, Y.,Kamitori, S.
Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis
CARBOHYDR.RES., 338:1553-1558, 2003

PubMed Abstract: Thermoactinomyces vulgaris R-47 produces two alpha-amylases, TVAI and TVAII, differing in substrate specificity from each other. TVAI favors high-molecular-weight substrates like starch, and scarcely hydrolyzes cyclomaltooligosaccharides (cyclodextrins) with a small cavity. TVAII favors low-molecular-weight substrates like oligosaccharides, and can efficiently hydrolyze cyclodextrins with various sized cavities. To understand the relationship between the structure and substrate specificity of these enzymes, we precisely examined the roles of key residues for substrate recognition by X-ray structural and kinetic parameter analyses of mutant enzymes and successfully obtained mutants in which the substrate specificity of each enzyme is partially converted into that of another.

PubMed: 12860426
DOI: 10.1016/S0008-6215(03)00219-2

実験手法

X-RAY DIFFRACTION (2.2 Å)