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
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
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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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