Department of Chemistry, Biotechnology, and Food Science, The Norwegian University of Life Sciences (NMBU), P.O. Box 5003, 1432 Ås, Norway.
Department of Chemistry, Biotechnology, and Food Science, The Norwegian University of Life Sciences (NMBU), P.O. Box 5003, 1432 Ås, Norway.
Curr Opin Struct Biol. 2017 Jun;44:67-76. doi: 10.1016/j.sbi.2016.12.012. Epub 2017 Jan 10.
Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of glycosidic bonds and represent a promising resource for development of industrial enzyme cocktails for biomass processing. LPMOs show high sequence and modular diversity and are known, so far, to cleave insoluble substrates such as cellulose, chitin and starch, as well as hemicelluloses such as beta-glucan, xyloglucan and xylan. All LPMOs share a catalytic histidine brace motif to bind copper, but differ strongly when it comes to the nature and arrangement of residues on the substrate-binding surface. In recent years, the number of available LPMO structures has increased rapidly, including the first structure of an enzyme-substrate complex. The insights gained from these structures is reviewed below.
溶细胞多糖单加氧酶（LPMOs）催化糖苷键的氧化裂解，是开发用于生物质处理的工业酶制剂的有前途的资源。LPMOs 表现出高度的序列和模块多样性，迄今为止已知它们可以切割不溶性底物，如纤维素、壳聚糖和淀粉，以及半纤维素，如β-葡聚糖、木葡聚糖和木聚糖。所有 LPMOs 都具有一个催化组氨酸支架基序来结合铜，但在底物结合表面上的残基的性质和排列上存在很大差异。近年来，可用的 LPMO 结构数量迅速增加，包括第一个酶-底物复合物的结构。下面综述了从这些结构中获得的见解。
