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When substrates change the shape of the active sites in enzymes in order to activate them
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How does the induced fit model help to explain non-competitive inhibition?
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.
What is a induced fit hypothesis?
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.
How are the ''lock and key'' and ''induced fit'' models similar?
bontot
Define the enzyme-substrate complex?
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.
What is a change in the shape of an enzyme allowing it to react effectively with a substrate is a what?
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.
How the lock and key model and the induced fit model differ?
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.
Why is the Induced fit model better than the lock and key model?
induce fit model is better because it causes a change in the enzyme active sit and allows the substrate to fit in
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Adam Kleppner has written: 'The notion of induced representations' -- subject(s): Group theory
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As an enzyme fits into a substrate at the active site it undergoes a slight change in order to fit into the substrate. this process is defined by a concept called?
This concept is called an induced fit.
