Potassium ion-dependent trehalose phosphorylase from halophilic Bacillus selenitireducens MLS10
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- 作者：Takanori Nihira ; Yuka Saito ; Kazuhiro Chiku ; Motomitsu Kitaoka ; Ken¡¯ichi Ohtsubo ; Hiroyuki Nakai
- 关键词：ABC ; ATP-binding cassette ; GH ; glycoside hydrolase family ; ¦ÂGlc1P ; ¦Â-d-glucose 1-phosphate ; HEPES ; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid ; PAGE ; polyacrylamide-gel electrophoresis ; PTS ; phosphoenolpyruvate ; carbohydrate phosphotransferase
- 刊名：FEBS Letters
- 出版年：2013
- 出版时间：1 November, 2013
- 年：2013
- 卷：587
- 期：21
- 页码：3382-3386
- 全文大小：622 K
文摘
We discovered a potassium ion-dependent trehalose phosphorylase (Bsel_1207) belonging to glycoside hydrolase family 65 from halophilic Bacillus selenitireducens MLS10. Under high potassium ion concentrations, the recombinant Bsel_1207 produced in Escherichia coli existed as an active dimeric form that catalyzed the reversible phosphorolysis of trehalose in a typical sequential bi bi mechanism releasing ¦Â-d-glucose 1-phosphate and d-glucose. Decreasing potassium ion concentrations significantly reduced thermal and pH stabilities, leading to formation of inactive monomeric Bsel_1207.