Pg:- 70,71,72,73
Ch:- 5
Enzyme action describes how enzymes function as biological catalysts to speed up chemical reactions in living organisms. They do this by lowering the activation energy required for a reaction, making the process faster and more efficient.
Substrate Binding:
Enzymes bind to specific molecules called substrates. This occurs at the enzyme's active site, a specially shaped region that matches the substrate's shape. This interaction can be explained by two models:
Lock and Key Model: The substrate fits the enzyme like a key fits into a lock.
Induced Fit Model: The enzyme changes shape slightly to better accommodate the substrate.
Formation of the Enzyme-Substrate Complex:
Once the substrate binds to the active site, an enzyme-substrate complex is formed. This temporary complex aligns the substrate molecules in a way that facilitates the reaction.
Catalysis:
The enzyme catalyzes the conversion of substrates into products. It achieves this by:
Lowering activation energy: Reducing the energy barrier needed for the reaction to proceed.
Stabilizing transition states: Making intermediate stages of the reaction more stable.
Product Formation:
The chemical reaction takes place, and the substrate is transformed into the final product(s). For example:
Hydrolysis: Breaking down a molecule into smaller parts (e.g., breaking a protein into amino acids).
Synthesis: Joining smaller molecules into a larger product.
Product Release:
After the reaction, the enzyme releases the product(s) from the active site. The enzyme itself remains unchanged and can catalyze additional reactions.
Recycling:
The enzyme is free to repeat the process with new substrate molecules. This makes enzymes highly efficient—they can catalyze many reactions without being consumed.
Factors Affecting Enzyme Action:
Several factors influence how well enzymes function:
Temperature: Too high or too low can denature the enzyme or slow its activity.
What is the role of cofactors and coenzymes in enzyme activity?
How do temperature and pH affect enzyme activity and stability?
What is the difference between competitive and non-competitive inhibition of enzymes?
How do allosteric enzymes regulate metabolic pathways?
What are some examples of enzymes involved in key biochemical processes, such as digestion and DNA replication?
How are enzymes used in industrial applications, such as biotechnology and medicine?
What are the methods used to study and measure enzyme kinetics?
1. Describe the role of the enzyme's active site in substrate binding. How does the shape of the active site determine the enzyme's specificity for its substrate?
2. Explain the difference between the Lock and Key Model and the Induced Fit Model of enzyme-substrate interaction. Provide an example of each model from biological reactions.
3. Consider an enzyme that breaks down proteins. Explain how hydrolysis works in this context and how the enzyme speeds up this reaction.
4. What happens to an enzyme after the products are released from the active site? How does this process contribute to the enzyme's efficiency?