AI Article Synopsis
- Researchers identified a potassium ion-dependent trehalose phosphorylase (Bsel_1207) from the salt-loving bacteria Bacillus selenitireducens MLS10, classified under glycoside hydrolase family 65.
- In high potassium environments, the enzyme functions as an active dimer, efficiently breaking down trehalose through a reversible reaction that produces β-D-glucose 1-phosphate and D-glucose.
- Lowering potassium levels negatively impacts the enzyme's stability against heat and pH changes, causing it to convert into an inactive monomer form.
Article 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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| http://dx.doi.org/10.1016/j.febslet.2013.08.038 | DOI Listing |
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