5M99

Functional Characterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization

5M99 の概要

• エントリーDOI: 10.2210/pdb5m99/pdb
• 分子名称: Alpha-amylase, SODIUM ION, POTASSIUM ION, ... (8 entities in total)
• 機能のキーワード: hydrolase glycosyl hydrolase 13 family alpha amylase activity, hydrolase
• 由来する生物種: Thermotoga petrophila RKU-1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 120597.68

構造登録者

Hameed, U.,Price, I.,Mirza, O.A. (登録日: 2016-11-01, 公開日: 2017-07-19, 最終更新日: 2024-05-08)

主引用文献

Hameed, U.,Price, I.,Ke, A.,Wilson, D.B.,Mirza, O.
Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization.
Biochim. Biophys. Acta, 1865:1237-1245, 2017

PubMed Abstract: Thermostable α-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative α-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100°C, with optimum activity at 98°C and pH8.5. The activity increased in the presence of Rb, K and Ca ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7Å resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases.

PubMed: 28648523
DOI: 10.1016/j.bbapap.2017.06.015

実験手法

X-RAY DIFFRACTION (1.96 Å)