3BSG

Barley alpha-amylase isozyme 1 (AMY1) H395A mutant

3BSG の概要

• エントリーDOI: 10.2210/pdb3bsg/pdb
• 関連するPDBエントリー: 1HT6 3BSH
• 分子名称: Alpha-amylase type A isozyme, CALCIUM ION (3 entities in total)
• 機能のキーワード: barley alpha-amylase, amy1, mutant, calcium, carbohydrate metabolism, germination, glycosidase, hydrolase, metal-binding, secreted
• 由来する生物種: Hordeum vulgare (Barley)
• 細胞内の位置: Secreted, extracellular space: P00693
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45550.17

構造登録者

Aghajari, N.,Robert, X.,Haser, R. (登録日: 2007-12-24, 公開日: 2008-08-26, 最終更新日: 2023-11-01)

主引用文献

Nielsen, M.M.,Seo, E.S.,Bozonnet, S.,Aghajari, N.,Robert, X.,Haser, R.,Svensson, B.
Multi-site substrate binding and interplay in barley alpha-amylase 1
Febs Lett., 582:2567-2571, 2008

PubMed Abstract: Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and Y105A/Y380M show that each of Tyr380 and Tyr105 is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr105 predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants.

PubMed: 18588886
DOI: 10.1016/j.febslet.2008.06.027

実験手法

X-RAY DIFFRACTION (1.95 Å)