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首页> 外文期刊>Chemistry: A European journal >NMR spectroscopic analysis reveals extensive binding interactions of complex xyloglucan oligosaccharides with the Cellvibrio japonicus glycoside hydrolase family 31 α-xylosidase
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NMR spectroscopic analysis reveals extensive binding interactions of complex xyloglucan oligosaccharides with the Cellvibrio japonicus glycoside hydrolase family 31 α-xylosidase

机译：NMR光谱分析显示复杂的木葡聚糖寡糖与Cellvibrio japonicus糖苷水解酶家族31α-木糖苷酶的广泛结合相互作用

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摘要

The study of the interaction of glycoside hydrolases with their substrates is fundamental to diverse applications in medicine, food and feed production, and biomass-resource utilization. Recent molecular modeling of the α-xylosidase CjXyl31A from the soil saprophyte Cellvibrio japonicus, together with protein crystallography and enzyme-kinetic analysis, has suggested that an appended PA14 protein domain, unique among glycoside hydrolase family 31 members, may confer specificity for large oligosaccharide fragments of the ubiquitous plant polysaccharide xyloglucan (J. Larsbrink, A. Izumi, F. M. Ibatullin, A. Nakhai, H. J. Gilbert, G. J. Davies, H. Brumer, Biochem. J. 2011, 436, 567-580). In the present study, a combination of NMR spectroscopic techniques, including saturation transfer difference (STD) and transfer NOE (TR-NOE) spectroscopy, was used to reveal extensive interactions between CjXyl31A active-site variants and xyloglucan hexa- and heptasaccharides. The data specifically indicate that the enzyme recognizes the entire cello-tetraosyl backbone of the substrate and product in positive enzyme subsites and makes further significant interactions with internal pendant α-(1→6)-linked xylosyl units. As such, the present analysis provides an important rationalization of previous kinetic data on CjXyl31A and unique insight into the role of the PA14 domain, which was not otherwise obtainable by protein crystallography.
机译：糖苷水解酶与其底物相互作用的研究是医学，食品和饲料生产以及生物质资源利用中各种应用的基础。最近来自土壤腐生植物日本弧菌的α-木糖苷酶CjXyl31A的分子建模，以及蛋白质晶体学和酶动力学分析表明，在糖苷水解酶家族31个成员中独特的附加PA14蛋白结构域可赋予大寡糖片段特异性无处不在的植物多糖木葡聚糖（J.Larsbrink，A.Izumi，FM Ibatullin，A.Nakhai，HJ Gilbert，GJ Davies，H.Brumer，Biochem.J.2011，436，567-580）。在本研究中，结合使用NMR光谱技术，包括饱和转移差异（STD）和转移NOE（TR-NOE）光谱，揭示CjXyl31A活性位点变体与木葡聚糖六糖和七糖之间的广泛相互作用。数据具体表明，该酶在正酶亚位点识别底物和产物的整个纤维-四糖基骨架，并与内部侧链α-（1→6）连接的木糖基单元进行进一步的显着相互作用。这样，本分析为CjXyl31A上的先前动力学数据提供了重要的合理化依据，并提供了对PA14结构域作用的独特见解，而PA14结构域则无法通过蛋白质晶体学获得。

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