Levansucrase of Bacillus subtilis. Characterization of a form isolated from phenol-treated cells and activated by Triton X-100.
A macromolecular complex including an inactive and protease-sensitive form of levansucrase was isolated from phenol treatment of Bacillus subtilis. This complex has a weak affinity for hydroxyapatite. Its molecular weight is evaluated at 300 000. This levansucrase form may be activated either by Triton X-100, above its critical micellar concentration, or by phospholipase C. The enzyme form associated with the complex is quite different from the exocellular levansucrase, which is protease-insensitive and detergent-insensitive, shows high affinity for hydroxyapatite and has a molecular weight of 54 000. Triton X-100 disaggregates this complex. The active levansucrase released becomes protease-insensitive and has the same apparent sedimentation coefficient as the exocellular enzyme. Possible relationships between the existence of this trapped complex and the secretion process of levansucrase are discussed.
D001412:Bacillus subtilis / Q000201:enzymology*; D002845:Chromatography; D004789:Enzyme Activation; D006602:Hexosyltransferases / Q000302:isolation & purification*; D006882:Hydroxyapatites; D008970:Molecular Weight; D009994:Osmolar Concentration; D010447:Peptide Hydrolases / Q000378:metabolism; D010636:Phenols / Q000494:pharmacology; D010740:Phospholipases / Q000378:metabolism; D011092:Polyethylene Glycols / Q000494:pharmacology
D006882:Hydroxyapatites; D010636:Phenols; D011092:Polyethylene Glycols; D006602:Hexosyltransferases; C021513:levansucrase; D010740:Phospholipases; D010447:Peptide Hydrolases