the answer is lock and key model .
The model you are referring to is the lock-and-key model of enzyme-substrate interaction. This model proposes that enzymes have specific active sites that perfectly fit the substrate, similar to how a lock fits a key. This precise fit allows for the formation of the enzyme-substrate complex and subsequent catalysis of the reaction.
A common and effective way to illustrate the interaction of an enzyme with another molecule is through a lock-and-key model or induced fit model. In the lock-and-key model, the enzyme has a specific active site that fits the substrate like a key into a lock. The induced fit model suggests that the enzyme undergoes a conformational change to better accommodate the substrate. Both models help visualize the specificity and mechanism of enzyme-substrate interactions.
in order to explain the mechanism of enzymes action a German chemist Emil fischer,in 184,proposed the lock and key model.According to this model both the enzymes and the substrate possess specific complementary geometric shapes that fit exactly into one another.This model explain enzyme specificity.
The specific property of an enzyme reaction demonstrated by the paper clip model in Augusto's dream is lowering the activation energy required for the reaction to occur. This is symbolized by the paper clip (enzyme) bringing the ends of the paper together (catalyzing the reaction) with less force or energy needed.
This concept is known as the induced fit model of enzyme-substrate interaction. It proposes that the active site of an enzyme can change its shape slightly to better accommodate the substrate, leading to optimal binding and catalysis. The binding of the substrate induces a conformational change in the enzyme, enhancing its activity.
The induced fit model is considered better than the lock and key model because it takes into account the dynamic nature of enzymes and substrates, allowing for more flexibility in enzyme-substrate interactions. This model suggests that both enzyme and substrate undergo conformational changes to better fit each other, resulting in higher specificity and efficiency of the enzyme-substrate complex. Overall, the induced fit model provides a more accurate representation of the enzyme-substrate interaction compared to the rigid lock and key model.
In a model of enzyme action, the enzyme can attach only to a substrate (reactant) with a specific shape. The enzyme then changes and reduces the activation energy of the reaction so reactants can become products. The enzyme is unchanged and is available to be used again.
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The lock and key model means that the substrate must perfectly fit the enzyme, and the enzyme does not change. The induced fit model is different as when the substrate fits together with the enzyme, the enzyme itself will change to either join substrates together or break a substrate down.
The model you are referring to is the lock-and-key model of enzyme-substrate interaction. This model proposes that enzymes have specific active sites that perfectly fit the substrate, similar to how a lock fits a key. This precise fit allows for the formation of the enzyme-substrate complex and subsequent catalysis of the reaction.
enzymes work on lock and key model and induced fit model.
A common and effective way to illustrate the interaction of an enzyme with another molecule is through a lock-and-key model or induced fit model. In the lock-and-key model, the enzyme has a specific active site that fits the substrate like a key into a lock. The induced fit model suggests that the enzyme undergoes a conformational change to better accommodate the substrate. Both models help visualize the specificity and mechanism of enzyme-substrate interactions.
The lock-and-key model provides a useful illustration of how an enzyme interacts with a substrate molecule. In this model, the enzyme's active site is complementary in shape to the substrate, similar to a key fitting into a lock. This specificity allows for efficient catalysis of the reaction.
To determine the optimum pH of an enzyme, you can conduct experiments at different pH levels and measure the enzyme activity. The pH at which the enzyme shows the highest activity is considered its optimum pH.
The two models are the lock-and-key model, where the substrate fits perfectly into the enzyme's active site like a key in a lock, and the induced fit model, where the active site of the enzyme changes its shape slightly to accommodate the substrate upon binding.
ALL enzymes use the lock and key model!