Institute of Biochemistry and Biotechnology, University of the Punjab, Lahore, Pakistan.
Faculty of Chemistry, Biotechnology, and Food Science, The Norwegian University of Life Sciences (NMBU), Ås, Norway.
FEBS Lett. 2018 Aug;592(15):2562-2571. doi: 10.1002/1873-3468.13189. Epub 2018 Jul 26.
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 BcLPMO10A). We show that BcLPMO10A, 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. BcLPMO10A enhances the activity of chitinases during the degradation of α-chitin.
溶细胞多糖单加氧酶（LPMOs）有助于将甲壳素和纤维素等难处理的多糖进行酶促转化，并且在细菌感染中可能也发挥作用。一些 LPMOs 是多模块的，其含义仍部分未知。我们研究了来自食物中毒细菌蜡样芽孢杆菌（命名为 BcLPMO10A）的四模块 LPMO 的性质。我们表明，BcLPMO10A 由一个 LPMO 结构域、两个纤维连接蛋白型 III（FnIII）样结构域和一个碳水化合物结合模块（CBM5）组成，是一种强大的甲壳素活性 LPMO。虽然 FnIII 结构域的作用仍不清楚，但我们表明，酶功能强烈依赖于 CBM5，CBM5 通过促进底物结合，保护酶免于失活。BcLPMO10A 在 α-壳聚糖的降解过程中增强几丁质酶的活性。
