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热等离子体酸性的功能状态依赖于一种额外的碳素终端序列

Leticia Ramírez-Silva¹, Héctor Riveros-Rosas¹, Gloria Hernández-Alcántara¹

¹Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México 04510, Mexico.

International journal of molecular sciences

|September 13, 2025

概括

在Thermoplasma acidophilum pyruvate kinase中,额外的C终端序列 (ECTS) 对于其活性四重体状态和酶活性至关重要. 删除这个序列会产生一个聚合的,不活跃的酶,突出显示ECTS.

科学领域:

生物化学生物化学
结构生物学结构生物学
酶学是一种酶学.

背景情况:

酸盐激酶酶在遗传学上被分为K + 依赖和K + 独立的组.
热等离子体酸酸酸激酶,尽管是K + 独立的,但与K + 依赖的酶共享保留的特征.
这些酶组之间存在着不同的催化机制.

研究的目的:

调查额外的C终端序列 (ECTS) 在T. acidophilum pyruvate kinase的活性构造中的作用.
了解这个古老的酶是如何实现其功能结构的.

主要方法:

结构建模以确定ECTS.
构建和比较野生类型和截断 (缺乏ECTS) 的T. acidophilum pyruvate kinase.
对运动参数,远紫外线CD光谱,热稳定性,分子动力学模拟和寡合体状态的分析.

主要成果:

截断的酶是聚合的,活性明显较低,并且存在于较小的寡合体状态.
野生类型的酶保持一个活跃的四重体状态.
为了保持活跃的四重体构成和酶功能,ECTS是必不可少的.

结论:

该ECTS对于T. acidophilum pyruvate kinase的稳定性和活性至关重要.
这种在其他古生物和细菌中发现的序列,可能代表一个古老的,潜在的不稳定域.
据报道,ECTS是首次报告的古老的pyruvate kinase序列,为酶进化提供了洞察力.

关键词:

热等离子体酸性 (Thermoplasma acidophilum) 是一种热等离子体.额外的炭基末端序列.动力常数是动力常数.酸激酶是一种酸激酶.四分制结构的四分制结构.

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