Characterization and synergistic action of a tetra‐modular lytic polysaccharide monooxygenase from Bacillus cereus. Issue 15 (26th July 2018)

• Record Type: Journal Article
• Authors: Mutahir, Zeeshan; Mekasha, Sophanit; Loose, Jennifer S. M.; Abbas, Faiza; Vaaje‐Kolstad, Gustav; Eijsink, Vincent G. H.; Forsberg, Zarah
• Is Part Of: FEBS letters. Volume 592:Issue 15(2018)
• Page Start: 2562
• Page End: 2571
• Publication Date: 2018-07-26
• Subjects: chitin -- LPMO -- multimodular; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13189
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Lytic polysaccharide monooxygenases (LPMOs) contribute to enzymatic conversion of recalcitrant polysaccharides such as chitin and cellulose and may also play a role in bacterial infections. Some LPMOs are multimodular, the implications of which remain only partly understood. We have studied the properties of a tetra‐modular LPMO from the food poisoning bacterium Bacillus cereus (named Bc LPMO10A). We show that Bc LPMO10A, comprising an LPMO domain, two fibronectin‐type III (FnIII)‐like domains, and a carbohydrate‐binding module (CBM5), is a powerful chitin‐active LPMO. While the role of the FnIII domains remains unclear, we show that enzyme functionality strongly depends on the CBM5, which, by promoting substrate binding, protects the enzyme from inactivation. Bc LPMO10A enhances the activity of chitinases during the degradation of α‐chitin. Abstract :