Potassium ion-dependent trehalose phosphorylase from halophilic Bacillus selenitireducens MLS10

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.

Keywords: 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid; ABC; ATP-binding cassette; Bacillus selenitireducens; GH; Glycoside hydrolase family 65; HEPES; PAGE; PTS; Potassium ion-dependent; Trehalose phosphorylase; glycoside hydrolase family; phosphoenolpyruvate: carbohydrate phosphotransferase; polyacrylamide-gel electrophoresis; β-d-glucose 1-phosphate; βGlc1P.