高温要求中的其他决定因素 一种酶被保存并调节活跃构造的种群
Arvind Kumar Gupta1, Kushal Singh2, Yogesh Patidar3
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
ACS chemical biology
|June 15, 2023
概括
在高温要求的A (HtrA) 酶中保存的间残留网络控制着全调节. 扰乱这个网络会改变蛋白酶活性和 conformational 采样,支持一个整体全模型.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 高温要求的A (HtrA) 酶是全调节的蛋白酶.
- 效应因子与PDZ域结合,可以启动HtrA酶中的蛋白质分解活性.
- 整个HtrA酶的全性间残留网络的保存尚未得到充分理解.
研究的目的:
- 研究在HtrA酶中调控全菌的相互残留相互作用网络.
- 确定这些全网络是否在不同的HtrA同类体中得到保存.
- 工程突变扰乱了*M.结核病*HtrA.中的全卵性和形状采样.
主要方法:
- 对大肠杆菌 DegS 和结核病 M. PepD. 的分子动力学模拟.
- 在 *M.结核病* HtrA. 中的局部定向突变发生.
- 电子显微镜和X射线晶体学.
- 分析电子密度和组合建模.
主要成果:
- 在HtrA酶中确定了保存的残留物间相互作用网络.
- 在 *M.结核病* HtrA 中的突变扰乱了全调节和活性位点拓.
- 实验数据显示,突变影响了 conformational 采样,影响了具有催化能力的活性部位.
- 在DegS的突变证实了保留残留在全反应中的作用.
结论:
- 控制HtrA异质的相互残留网络在同类物体中保持一致.
- 这个网络的扰乱会改变构造性采样和全反应.
- 一个整体全模型有效地描述了HtrA酶中受调节的蛋白质分解.
相关概念视频
01:13Introduction to Mechanisms of Enzyme Catalysis
8.3K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
8.3K
01:19Allosteric Proteins-ATCase
5.8K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.8K
01:29Diversity of Archaea IV
58
Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist...
58
01:27Diversity of Archaea III
33
Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like...
33
01:08Allosteric Regulation
58.3K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
58.3K
02:28Effect of Temperature Change on Reaction Rate
4.2K
The Arrhenius equation,
4.2K