Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
J Am Chem Soc. 2012 May 16;134(19):8030-3. doi: 10.1021/ja301334b. Epub 2012 May 2.
Protein endoglycosidases are useful for biocatalytic alteration of glycans on protein surfaces, but the currently limited selectivity of endoglycosidases has prevented effective manipulation of certain N-linked glycans widely found in nature. Here we reveal that a bacterial endoglycosidase from Streptococcus pyogenes , EndoS, is complementary to other known endoglycosidases (EndoA, EndoH) used for current protein remodeling. It allows processing of complex-type N-linked glycans +/- core fucosylation but does not process oligomannose- or hybrid-type glycans. This biocatalytic activity now addresses previously refractory antibody glycoforms.
蛋白内切糖苷酶可用于生物催化改变蛋白表面的聚糖，但目前内切糖苷酶的选择性有限，无法有效操纵自然界中广泛存在的某些 N 连接聚糖。在这里，我们发现化脓性链球菌的一种细菌内切糖苷酶 EndoS 与用于当前蛋白质重塑的其他已知内切糖苷酶（EndoA、EndoH）互补。它允许加工复杂型 N 连接聚糖 +/-核心岩藻糖基化，但不加工寡甘露糖型或杂合型聚糖。这种生物催化活性现在可以解决以前难以处理的抗体糖型。
