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首页> 外文期刊>FEMS Microbiology Letters >An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans
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An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans

机译:粪肠球菌V583的内切β-N-乙酰氨基葡萄糖苷酶,负责水解高甘露糖和杂合型N-连接聚糖

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摘要

It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain. We have analyzed the other candidate, EF2863, and show that this predicted single domain GH18 protein is an endo-β-N-acetylglucosaminidase. EF2863 hydrolyzes the glycosidic bond between two N-acetylglucosamines (GlcNAc) in N-linked glycans of the high-mannose and hybrid type, releasing the glycan and leaving one GlcNAc attached to the protein. The activity of EF2863 is similar to that of the well known deglycosylating enzyme EndoH from Streptomyces plicatus. According to the CAZy nomenclature, the enzyme is designated EfEndo18A.
机译:先前已证明粪肠球菌产生分泌的糖苷内切酶,使细菌能够从糖蛋白中去除N-连接的聚糖。可能负责这种活性的一种酶是EF0114,其包含典型的GH18内切糖苷酶结构域和GH20结构域。我们已经分析了另一种候选药物EF2863,并表明该预测的单结构域GH18蛋白是内切β-N-乙酰氨基葡糖苷酶。 EF2863水解高甘露糖和杂合型N联聚糖中两个N-乙酰氨基葡糖胺(GlcNAc)之间的糖苷键,释放出聚糖,并使一个GlcNAc附着在蛋白质上。 EF2863的活性类似于褶皱链霉菌的众所周知的去糖基化酶EndoH的活性。根据CAZy命名法,该酶称为EfEndo18A。

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