Single amino acid residue changes in subsite-1 of levansucrase from Zymomonas mobilis 10232 strongly influence the enzyme activities and products

文献类型： 外文期刊

第一作者： Li, Shuying

作者： Li, Shuying;Yan, Yongliang;Zhou, Zhengfu;Yu, Haiying;Zhan, Yuhua;Zhang, Wei;Chen, Ming;Lu, Wei;Ping, Shuzhen;Lin, Min

作者机构：

关键词： sucrose: 57-50-1;oligosaccharide;amino acid;levan: 9013-95-0;inulosucrase: 9030-16-4;EC 2.4.1.9;enzyme activity

期刊名称：MOLECULAR BIOLOGY REPORTS （ 影响因子：2.316； 五年影响因子：2.357 ）

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年卷期：

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收录情况： SCI

摘要： The -1 subsite of bacterial fructansucrases (FSs) (levansucrases and inulosucrases) plays an important role in the substrate recognition, binding and catalysis. Three residues (for example W47, W118 and R193, Zymomonas mobilis levansucrase numbering) at the -1 subsite are completely conserved among FSs. Site-directed mutational analysis showed that the substitutions of the three strictly conserved amino acid residues, W47N, W47H, W118N, W118H, R193K and R193H, significantly decreased enzyme activities and synthesis rates of levan, while the size of the synthesized oligosaccharides had been influenced. These experimental results, combined with 3D structure modeling, lead to our proposal that a single amino acid residue change in subsite -1 of levansucrase can influence change to the size and polarity of the sucrose binding pocket with a concomitant change to substrate binding and catalysis, and thus having an overall influence on the enzyme activities and products.

分类号： Q7

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