According to lock and key model both the enzymes and the substrate possess specific geometrical shapes that fit exactly into one another.
WHILE
According to the induced fit model enzymes are more flexible structures and their active site is reshaped as substrate interacts with the enzymes.
The induced fit model is the theory that instead of enzymes and substrates fitting exactly together, as in the lock and key model, the enzyme changes shape around the substrate to bind with it. Non-competitive inhibition is where the inhibitor does not fit into the active site, but into another site on the enzyme instead, which changes the shape of the active site.
a. The substrate can be altered so it is induced to fit into the enzyme's active site. b. The enzyme changes its shape slightly as it binds to the substrate. c. The enzyme is altered so it is induced to fit many different types of substrate. d. Several sites on an enzyme can be induced to act on a substrate.
Scientific ideas are modified when evidence is found that does not fit the predictions. The scientists determine why and revise the model to fit the new data.
Keys can be distinguished by several characteristics, including their shape, size, material, and the specific patterns or grooves cut into their shafts. The unique arrangement of these cuts, known as the key's bitting, allows it to fit into and operate a particular lock. Additionally, keys may have distinct features such as notches or plastic covers that further differentiate them. Overall, these variations ensure that each key corresponds to its designated lock, enhancing security and functionality.
clearance Fit - if the clearance is more between the mating parts then it is known as clearance fit. Transition Fit- If the clearance is less between the mating parts then it is known as Transition fit Interference Fit- If the mating parts are fouling or interfering.then it is known as Interference Fit
enzymes work on lock and key model and induced fit model.
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 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.
The modification of the lock and key model that suggests the active site of an enzyme is known as the "induced fit model." This model proposes that while the active site of an enzyme has a specific shape (like a lock), it can undergo conformational changes upon substrate binding (like a key adjusting to fit the lock). This flexibility allows for a more precise interaction between the enzyme and its substrate, enhancing catalytic efficiency. The induced fit model highlights the dynamic nature of enzyme-substrate interactions compared to the rigidity of the original lock and key model.
The key and lock theory suggests that enzymes and substrates fit together like a key fits into a lock with a rigid, non-flexible active site. In contrast, the induced fit model proposes that the enzyme's active site can change its shape to accommodate the substrate, thus providing a more dynamic interaction between the enzyme and substrate.
Both the lock and key and induced fit models describe how enzymes interact with substrates to facilitate biochemical reactions. In the lock and key model, the enzyme's active site is a perfect fit for a specific substrate, much like a key fitting into a lock. In contrast, the induced fit model suggests that the enzyme's active site is flexible and can change shape to better accommodate the substrate upon binding. Despite these differences, both models emphasize the importance of the enzyme-substrate interaction in catalyzing reactions.
the answer is lock and key model .
bontot
Both the lock and key model and induced fit model are mechanisms used to describe enzyme-substrate interactions. Both models explain how enzymes bind to substrates to facilitate chemical reactions. They both highlight the specificity of enzyme-substrate interactions.
The induced fit model is the theory that instead of enzymes and substrates fitting exactly together, as in the lock and key model, the enzyme changes shape around the substrate to bind with it. Non-competitive inhibition is where the inhibitor does not fit into the active site, but into another site on the enzyme instead, which changes the shape of the active site.
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 induced-fit model builds upon the lock and key theory by emphasizing that both the enzyme and substrate undergo conformational changes upon binding to each other. This model suggests that the enzyme's active site can actually change shape to accommodate the substrate more effectively, resulting in a tighter fit and enhancing catalytic efficiency.