Multiple rewards from a treasure trove of novel glycoside hydrolase and polysaccharide lyase structures: new folds, mechanistic details, and evolutionary relationships
Multiple rewards from a treasure trove of novel glycoside hydrolase and polysaccharide lyase structures: new folds, mechanistic details, and evolutionary relationships
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DOI：
10.1016/j.sbi.2013.06.001
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发表时间：
2013-10-01
影响因子：
6.8
通讯作者：
Coutinho, Pedro M.
中科院分区：
文献类型：
--
作者：
Fushinobu, Shinya;Alves, Victor D.;Coutinho, Pedro M.
综述了糖苷水解酶(GHS)和多糖裂解酶(PLs)的三维结构分析的最新进展。糖苷水解酶和多糖裂解酶是历史上与糖苷键断裂有关的两类酶。到目前为止，GH和PL家族中分别约有80%和95%具有代表性的晶体结构。作用于植物细胞壁多糖、鞘脂、血型抗原、牛奶低聚糖、N-葡聚糖、口腔生物膜和食用海藻的酶的新结构已被确定。一些生长激素酶有非常独特的催化残基，如天冬氨酸-希氏二聚体。高速原子力显微镜和计算模拟等新方法为研究这些酶的动力学和详细的分子相互作用开辟了一条途径。
Recent progress in three-dimensional structure analyses of glycoside hydrolases (GHs) and polysaccharide lyases (PLs), the historically relevant enzyme classes involved in the cleavage of glycosidic bonds of carbohydrates and glycoconjugates, is reviewed. To date, about 80% and 95% of the GH and PL families, respectively, have a representative crystal structure. New structures have been determined for enzymes acting on plant cell wall polysaccharides, sphingolipids, blood group antigens, milk oligosaccharides, N-glycans, oral biofilms and dietary seaweeds. Some GH enzymes have very unique catalytic residues such as the Asp-His dyad. New methods such as high-speed atomic force microscopy and computational simulation have opened up a path to investigate both the dynamics and the detailed molecular interactions displayed by these enzymes.