Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871056 | FEBS Letters | 2013 | 5 Pages |
Abstract
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 β-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.
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Authors
Takanori Nihira, Yuka Saito, Kazuhiro Chiku, Motomitsu Kitaoka, Ken'ichi Ohtsubo, Hiroyuki Nakai,