在酶中融合进化的范式
Ioannis G Riziotis1, Jenny C Kafas1, Gabriel Ong1
1European Bioinformatics Institute (EMBL-EBI), Cambridge, UK.
The FEBS journal
|November 22, 2024
概括
酶可以催化具有不同结构的相同反应,表明没有进化联系的功能融合. 这项研究分析了34个病例,揭示了酶功能的各种进化途径.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 进化生物学 进化生物学
背景情况:
- 催化相同反应的酶往往表现出不同的结构.
- 功能融合,即不相关的蛋白质进化类似的功能,是进化生物化学的一个关键领域.
- 机制和催化场地地图集 (M-CSA) 为研究酶功能和进化提供了丰富的资源.
研究的目的:
- 识别和分析酶功能融合的情况.
- 研究结构上不同的酶的进化独立性,这些酶催化相同的反应.
- 描述酶功能融合背后的序列,结构和机制特征.
主要方法:
- 利用M-CSA数据库识别了34个具有相同酶委员会号码但不同CATH折叠的酶病例.
- 对比这些酶对的序列,结构,活性部位几何,辅因子的使用和催化机制.
- 集成文献数据与计算资源 (M-CSA,PDBe,PDBsum) 和定制软件进行分析.
主要成果:
- 确定了34个具有明显折叠的酶之间功能融合的实例.
- 证明这些酶是独立进化的,可以进行相同的化学催化.
- 观察到多个不同的融合功能进化的模式.
结论:
- 酶的功能融合是一个反复出现的现象,具有不同的进化策略.
- 准确描述酶融合需要对序列,结构,活性部位和机制进行综合分析.
- 这项研究强调了整合结构数据库和计算工具以获得进化见解的力量.
相关概念视频
Convergent Evolution
27.6K
Evolution shapes the features of organisms over time, ensuring that they are suited for the environments in which they live. Sometimes, selection pressure leads to the rise of similar but unrelated adaptations in organisms with no recent common ancestors, a process known as convergent evolution.
27.6K
Catalytically Perfect Enzymes
3.9K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Most enzymes...
Most enzymes...
3.9K
Introduction to Enzymes
17.2K
The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
17.2K
Enzymes
80.8K
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...
80.8K
Introduction to Mechanisms of Enzyme Catalysis
8.0K
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...
8.0K
Enzyme Kinetics
96.0K
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...
96.0K


