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首页> 外文期刊>Biochemistry >Biochemical Characterization of the O-Linked Glycosylation Pathway in Neisseria gonorrhoeae Responsible for Biosynthesis of Protein Glycans Containing N,N '-Diacetylbacillosamine
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Biochemical Characterization of the O-Linked Glycosylation Pathway in Neisseria gonorrhoeae Responsible for Biosynthesis of Protein Glycans Containing N,N '-Diacetylbacillosamine

机译:淋病奈瑟氏球菌中O联糖基化途径的生物化学特性,负责生物合成包含N,N'-二乙酰基芽孢杆菌胺的蛋白质聚糖

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摘要

The O-linked protein glycosylation pathway in Neisseria gonorrhoeae is responsible for the synthesis of a complex oligosaccharide on undecaprenyl diphosphate and subsequent en bloc transfer of the glycan to serine residues of select periplasmic proteins. Protein glycosylation (pgl) genes have been annotated on the basis of bioinformatics and top-down mass spectrometry analysis of protein modifications in pgl-null strains [Aas, F. E., et al. (2007) Mol. Microbiol. 65, 607-624; Vik, A., et al. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 4447-4452], but relatively little biochemical analysis has been performed to date. In this report, we present the expression, purification, and functional characterization of seven Pgl enzymes. Specifically, the enzymes studied
机译:淋病奈瑟氏球菌中的O联蛋白糖基化途径负责在十一碳二烯基二磷酸上合成复杂的寡糖,随后将聚糖整体转移到所选周质蛋白的丝氨酸残基上。蛋白质糖基化(pgl)基因已根据生物信息学和pgl无效菌株中蛋白质修饰的自上而下质谱分析进行了注释[Aas,F. E.,et al。 (2007)Mol。微生物。 65,607-624; Vik,A。等。 (2009年)Proc。 Natl。学院科学U.S.A. 106,4447-4452],但是迄今为止,已经进行了相对较少的生化分析。在此报告中,我们介绍了七个Pgl酶的表达,纯化和功能表征。具体来说,研究的酶

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