Potassium ion-dependent trehalose phosphorylase from halophilic Bacillus selenitireducens MLS10.

Authors :: Nihira T
Saito Y
Chiku K
Kitaoka M
Ohtsubo K
Nakai H
Source :: FEBS letters [FEBS Lett] 2013 Nov 01; Vol. 587 (21), pp. 3382-6. Date of Electronic Publication: 2013 Sep 08.
Publication Year :: 2013
Abstract: We discovered a potassium ion-dependent trehalose phosphorylase (Bsel&#95;1207) belonging to glycoside hydrolase family 65 from halophilic Bacillus selenitireducens MLS10. Under high potassium ion concentrations, the recombinant Bsel&#95;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&#95;1207.<br /> (Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Subjects :: Bacillus metabolism
Bacterial Proteins chemistry
Cytoplasm metabolism
Escherichia coli metabolism
Genome, Bacterial
Glucosyltransferases chemistry
Hydrogen-Ion Concentration
Kinetics
Osmosis
Substrate Specificity
Temperature
Bacillus enzymology
Bacterial Proteins metabolism
Glucosyltransferases metabolism
Potassium metabolism

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