title: Reversible thermal unfolding of Bacillus subtilis levansucrase is modulated by Fe3+ and Ca2+.
abstract: The equilibrium transition curves for thermal unfolding of levansucrase were established at several pH values. At pH 7 and within the temperature range of bacterial growth, the unfolded form is predominant. However, under such conditions, refolding is promoted by the only addition of Ca2+ or Fe3+. We propose that the tertiary structure flexibility of levansucrase plays a key role in its secretion process.
authors: Institut Jacques Monod, CNRS, Université Paris VII, France.
authors: R
authors: R
authors: Chambert
authors: M F
authors: MF
authors: Petit-Glatron
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology*; D005290:Ferric Compounds / Q000494:pharmacology*; D006602:Hexosyltransferases / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation / Q000187:drug effects; D013050:Spectrometry, Fluorescence; D013381:Subtilisins / Q000494:pharmacology
chemical_list: D005290:Ferric Compounds; D006602:Hexosyltransferases; C021513:levansucrase; D013381:Subtilisins; D002118:Calcium