When substrates change the shape of the active sites in enzymes in order to activate them
The induced fit theory proposes that the active site of an enzyme changes its shape upon binding with the substrate. This change is induced by the interaction with the substrate, leading to a more precise fit and optimal conditions for catalysis to occur. This theory suggests that the binding of a substrate to an enzyme is a dynamic process rather than a static lock-and-key model.
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 a leadership theory that suggests a leader's effectiveness is determined by how well they help their followers achieve their goals by clarifying the path forward, removing obstacles, and providing necessary support and rewards. It focuses on how leaders can motivate followers to reach their objectives by adapting their leadership style to the needs and characteristics of their team.
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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.
bontot
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.
An induced fit is a change in the shape of an enzyme which allows it to react effectively with a substrate. The reason for the alteration is to speed up a chemical reaction.
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.
induce fit model is better because it causes a change in the enzyme active sit and allows the substrate to fit in
Geographic fit is evidence of the natural distribution and habitat preferences of a species. It can help researchers understand the range of environmental conditions that a species can thrive in and how it may respond to changes in its environment. Geographic fit evidence can also provide insights into the evolutionary history and dispersal patterns of a species.
Continental Drift Theory
Adam Kleppner has written: 'The notion of induced representations' -- subject(s): Group theory
A theory.
This concept is called an induced fit.