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首页> 外文期刊>Journal of Experimental Botany >Plant serpin protease inhibitors: specificity and duality of function
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Plant serpin protease inhibitors: specificity and duality of function

机译:植物筛选蛋白酶抑制剂:功能的特异性和二元性

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摘要

The serpins are a family of structurally conserved protease inhibitors found in all animal and plant kingdoms. After interaction with their cognate substrate(s), their native energetically stressed state is relaxed by hydrolysis, resulting in a semi-stable covalent bond that disables the protease. The inherent flexible serpin structure supports additional non-inhibitory functions. This review will focus on several biological functions attributed to plant serpins, ranging from specific cell death protease inhibitors to a stabilizing role for -amylase in seeds. Functional conservation of a particular serpin type, the LR serpins, is suggested by its compelling ubiquity throughout the plant kingdom. The multiple target specificity of plant serpins including the LR serpins enables them to perform dual functions that are not mutually exclusive both as a regulator of cell death and as a protective anti-pathogenic protein.
机译:蛇是在所有动物和植物王国中发现的结构保守蛋白酶抑制剂系列。 在与其同源底物相互作用后,通过水解缓和它们的天然能量应激状态,导致半稳定的共价键,其禁用蛋白酶。 固有的灵活Serpin结构支持额外的非抑制功能。 本综述将重点关注归因于植物血清的几种生物学功能,从特定的细胞死亡蛋白酶抑制剂到种子中的淀粉酶的稳定作用。 特定蛇素类型的功能守恒,LR Serpins,在整个植物王国中引人注目的ubiquity建议。 包括LR Serpins的植物蛇的多种靶特异性使得它们能够执行不作为细胞死亡调节剂和作为保护性抗致病蛋白相互关联的双重功能。

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