...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity
【24h】

Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity

机译：突变诱导的活性部位孔径根瘤菌sp.蔗糖异构酶水解活动

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Sucrose isomerase is an enzyme that catalyzes the production of sucrose isomers of high biotechnological and pharmaceutical interest. Owing to the complexity of the chemical synthesis of these isomers, isomaltulose and trehalulose, enzymatic conversion remains the preferred method for obtaining these products. Depending on the microbial source, the ratio of the sucrose-isomer products varies significantly. In studies aimed at understanding and explaining the underlying molecular mechanisms of these reactions, mutations obtained using a random-mutagenesis approach displayed a major hydrolytic activity. Two of these variants, R284C and F164L, of sucrose isomerase from Rhizobium sp. were therefore crystallized and their crystal structures were determined. The three-dimensional structures of these mutants allowed the identification of the molecular determinants that favour hydrolytic activity compared with transferase activity. Substantial conformational changes resulting in an active-site opening were observed, as were changes in the pattern of water molecules bordering the active-site region.
机译：蔗糖异构酶是一种催化的酶蔗糖产量高的同分异构体生物技术和制药的兴趣。由于化学合成的复杂性这些同分异构体,isomaltulose trehalulose,酶的转换仍然是首选方法获得这些产品。微生物源,sucrose-isomer的比值产品明显不同。在理解和解释的这些反应的分子机制,使用random-mutagenesis获得的突变方法显示主要的水解活性。两种变体,R284C F164L,蔗糖异构酶从根瘤菌sp.因此结晶和晶体结构测定。这些突变体的结构允许的识别分子的决定因素相比之下,有利于水解活动转移酶的活动。变化导致活性部位打开观察,水的模式的变化分子与活性部位地区接壤。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号