Distinct Interaction of Lytic Polysaccharide Monooxygenase with Cellulose Revealed by Computational and Biochemical Studies
Distinct Interaction of Lytic Polysaccharide Monooxygenase with Cellulose Revealed by Computational and Biochemical Studies
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计算和生化研究揭示了裂解多糖单加氧酶与纤维素的独特相互作用
DOI：
10.1021/acs.jpclett.0c00918
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发表时间：
2020
影响因子：
5.7
通讯作者：
Yin Heng
中科院分区：
文献类型：
--
作者：
Zhou Haichuan;Zhang Yuebin;Li Tang;Tan Haidong;Li Guohui;Yin Heng
一个独特的相互作用模式的溶解性多糖单加氧酶（LPMOs）与其不溶性底物，纤维素，揭示了通过计算和生物化学方法相结合。结果表明，该酶可通过位于跨保守的远端酪氨酸残基轴上的关键残基和铜离子与两个相邻的纤维素链相互作用，稳定地结合在纤维素平坦的疏水表面上。对底物结合与H2O2积累相关性的进一步研究表明，在实验室条件下，参与不溶性多糖生产性结合的LPMO不仅不能积累H2O2，而且还消耗未结合分子产生的H2O2。量子力学计算进一步证实了这一点。这些发现拓宽了我们对酶和不溶性底物之间相互作用的认识，加深了我们对H2O2在LPMO活性中所起作用的理解。
A distinct interaction pattern of lytic polysaccharide monooxygenases (LPMOs) with their insoluble substrate, cellulose, was revealed through the combination of computational and biochemical approaches. The results indicated that the enzymes can stably bind on the flat hydrophobic surface of cellulose via the interactions of the key residues located in the axis across the conserved distal tyrosine residue and copper ion with two adjacent cellulose chains. Further studies on the correlation of substrate binding and H2O2accumulation suggested that LPMOs involved in the productive binding on the insoluble polysaccharides not only fail to accumulate H2O2but also consume the H2O2produced by the unbound molecules under the lab condition. This was further substantiated by quantum-mechanical calculations. These findings broadened our knowledge of the interaction between enzymes and insoluble substrates and deepened our understanding of the role that H2O2plays in LPMO activity.