When substrates change the shape of the active sites in enzymes in order to activate them
An example of the induced fit theory is when an enzyme undergoes a conformational change to better accommodate the substrate upon binding. On the other hand, the lock and key theory suggests that the enzyme's active site is already in the correct shape to fit the substrate like a lock and key.
The lock and key theory of enzyme-substrate binding does not account for the induced fit model, where the enzyme and substrate can undergo conformational changes to better fit each other. It also does not explain the binding of substrates that are larger than the active site or the ability of enzymes to catalyze multiple types of reactions.
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.
Path-goal theory is about fit between motivation, behavior, environment, tasks, and reward (Evans, 1970; House, 1971). It traces its origins to expectancy theory, situational leadership and contingency theory, and builds upon all three. Path-goal theory is therefore about flexibility.
Strengths of situational theory include its focus on adapting leadership style to different situations, promoting flexibility and effectiveness. Limitations include the complexity of identifying and interpreting situational factors, and the challenge of constantly adjusting leadership approach to fit changing circumstances.
An example of the induced fit theory is when an enzyme undergoes a conformational change to better accommodate the substrate upon binding. On the other hand, the lock and key theory suggests that the enzyme's active site is already in the correct shape to fit the substrate like a lock and key.
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.
The lock and key theory and the induced fit theory are two theories that explain enzyme specificity. The lock and key theory proposes that the enzyme's active site is already in the correct shape to bind the substrate, like a key fitting into a lock. The induced fit theory suggests that the active site of the enzyme can change its shape slightly to accommodate the substrate, similar to a glove molding around a hand.
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.
This process is defined by a concept called induced fit. Induced fit is the dynamic process where the enzyme structure adjusts slightly to better accommodate and bind to the substrate molecule.
bontot
The lock and key theory of enzyme-substrate binding does not account for the induced fit model, where the enzyme and substrate can undergo conformational changes to better fit each other. It also does not explain the binding of substrates that are larger than the active site or the ability of enzymes to catalyze multiple types of reactions.
The theory of enzyme-substrate complex was established by Michaelis and Menton in 1913.According to their theory,enzyme combines with substrate to form enzyme-substrate complex.The transient complex has a lower energy of activation than that of substrate alone.This results in the acceleration of the reaction.The enzyme-substrate complex is broken down into enzyme and products of the reaction. E+S -ES - - -ES - - -E+P The different hypotheses of enzyme-substrate complex formation have been postulated.Early theory was postulated by Emil Fischer.According to this theory,the catalytic site of enzyme is preshaped to fit of the substrate.This hypothesis is called "lock and key" or rigid template.The next hypothesis has been proposed by Koshland in the late 1950s.The hypothesis was called "induced fit".Acccording to this theory,a catalytically active configuration of enzyme molecule and that of the active site can be induced only at the moment of attachment of the substate molecule,that is the substrate induces a conformotional change in the enzyme. At the present time,model of "induced fit" is modified.Binding the substrate with the enzyme leads not only to the conformational change of the protein molecule,but also to a geometrical and electrontopographic rearrangement of the substrate molecules. The modern "induced fit" hypothesis presumes the existence between the enzyme and the substrate of not only spatial or geometrical complementarity,but also electrostatic charge complementarity.
A change in the shape of an enzyme that allows it to better bind with a substrate is called induced fit. This conformational change occurs when the enzyme interacts with the substrate, forming a more complementary fit that enhances reaction efficiency.
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.
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.