在拥挤的环境中面向基酶的能量格局:活动,形状,结构和动态的顺序
Harshita Rastogi1, Arvind Singh1, Pramit K Chowdhury1
1Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, 110016, India.
Archives of biochemistry and biophysics
|June 1, 2023
概括
大分子拥挤影响腺酸激酶 (AK3L1) 酶的活性和结构. 群体增强域紧缩,并将最佳活性转移到更高的尿素度,影响酶动态.
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:
- 酶的功能依赖于复杂的结构变化和内部动态.
- 细胞环境的特点是巨分子拥挤,进一步复杂化了酶的行为.
- 在拥挤的条件下了解酶调节对于细胞过程至关重要.
研究的目的:
- 研究多域酶AK3L1 (腺酸激酶3 - 类似1) 的活性,结构,构造和动态之间的相互作用.
- 探索宏分子和化学化剂 (尿素) 如何调节酶的功能格局.
- 阐明影响AK3L1对拥挤环境中的干扰反应的因素.
主要方法:
- 基于振荡能量转移 (FRET) 的Förster域位移测量.
- 在亚纳秒时间解析的局部动态分析.
- 全球结构变化监测.
- 酶活性测定.酶活性测定.
- 在不同的尿素和宏分子度下进行的实验.
主要成果:
- AK3L1与尿素表现出双相行为:在低度下激活,在更高度下停用/展开.
- 大分子聚合物增强AK3L1域的紧缩,并转移最佳尿素度的活性.
- 酶活性和溶解动态的调节 (局部反应) 之前的全球展开.
- 活动地点的结构变化与大规模的全球转型脱而出.
结论:
- 大分子拥挤显著影响AK3L1的结构稳定性和酶活性.
- 酶对扰动的反应是顺序的,局部动态在全球展开之前.
- 从全球过渡中解脱活跃部位的变化表明,拥挤的细胞环境中存在复杂的调节机制.
相关概念视频
Protein Kinases and Phosphatases
13.2K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.2K
Enzymes
82.0K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
82.0K
Enzyme Kinetics
97.4K
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
97.4K
Introduction to Enzyme Kinetics
20.2K
Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
20.2K
ATP Synthase: Mechanism
14.8K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
14.8K
Introduction 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


