In an enzyme-catalyzed reaction, the reactant species to which the enzyme binds is called the substrate. The substrate is then converted into products by a series of steps. The lock-and-key model explains the steps involved in an enzyme-catalyzed reaction. Label the following diagram that illustrates the lock-and-key model of enzyme activity.
Drag the appropriate labels to their respective targets.
The Correct Answer and Explanation is :
It seems like you’ve provided a link to an image, but I can’t access external links. However, I can explain the lock-and-key model of enzyme activity and guide you in labeling the diagram based on this explanation.
Lock-and-Key Model of Enzyme Activity
In the lock-and-key model, the enzyme is compared to a lock, and the substrate to a key. The model suggests that the enzyme has a specific shape (the lock), and only the substrate (the key) with the complementary shape can fit into the enzyme’s active site.
Here are the key components you should look for when labeling the diagram:
- Substrate (Key): This is the reactant molecule that binds to the enzyme. It fits into the enzyme’s active site like a key fits into a lock. The substrate undergoes a chemical reaction once bound to the enzyme.
- Enzyme (Lock): The enzyme is a protein that catalyzes the reaction. It has a specific active site where the substrate binds. The enzyme itself doesn’t change during the reaction and can be reused.
- Active Site: This is the region on the enzyme where the substrate binds. It has a specific shape that matches the substrate, facilitating the reaction.
- Enzyme-Substrate Complex: Once the substrate binds to the enzyme’s active site, an enzyme-substrate complex is formed. This is the intermediate stage before the substrate is converted into products.
- Products: After the reaction takes place, the substrate is transformed into products. The products are released from the enzyme, allowing it to catalyze another reaction.
Explanation
The lock-and-key model illustrates enzyme specificity—only substrates with a complementary shape can bind to the enzyme’s active site. This model helps explain how enzymes are highly selective and efficient. The enzyme’s active site is rigid and only the right-shaped substrate can interact with it, much like how a key can only fit a particular lock.
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