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NONPRODUCTIVE BINDING
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Poor substrates bind to the enzyme in a large number of different ways, only one of which is correct Good substrates bind only in the proper way
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Again this model tells us why poor substrates don t work well Poor substrates bind more often to the enzyme in the wrong orientation than in the right orientation Since poor substrates bind in the wrong orientation, the catalytic groups and specific interactions that would accelerate the reaction of the correct substrate come into play in only a very small number of the interactions between the enzyme and a bad substrate In contrast to the induced-fit model, this model does not require a change in the conformation of the enzyme (Fig 7-4) In the hexokinase reaction discussed earlier, the nonproductive binding model would say that only 1 out of 105 water molecules binds to the enzyme in a productive fashion but all the glucose binds in a productive orientation
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Luckily, water is not a good substrate for hexokinase Otherwise, the ATP hydrolysis would burn up ATP
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Basic Concepts in Biochemistry
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BAD Substrate GOOD Substrate
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Enzyme in INACTIVE Conformation
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Enzyme in ACTIVE Conformation
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The INDUCED-FIT model for enzyme specificity says that good substrates must be able to cause the enzyme to change shape (conformation) so that catalytic and functional groups on the enzyme are brought into just the right place to catalyze the reaction Bad substrates are bad because they aren t able to make the specific interactions that cause the conformation change, and the enzyme stays in its inactive conformation
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Enzyme Mechanism
Good substrates bind to the enzyme in only the correct way
Bad substrates bind to the enzyme in a large number of incorrect, nonproductive ways
Figure 7-4
The NONPRODUCTIVE BINDING model suggests that while good substrates bind in only one, correct way, bad substrates usually bind to the enzyme incorrectly and cannot react
ENTROPY
Organizing a reaction at the active site of an enzyme makes it go faster When molecules react, particularly when it s the reaction between two different molecules or even when it s a reaction between two parts of the same molecule, they must become more organized The reason is that the two reacting atoms must approach each other in space Just finding the appropriate partner is often a tough part of the reaction (biochemistry mimics life once more) Part of the free-energy barrier to a chemical reaction is overcoming unfavorable entropy changes that must accompany the formation of the transition state By binding two substrates at the same active site, the enzyme organizes the reacting centers
Basic Concepts in Biochemistry
This reduces the amount of further organization that must occur to reach the transition state for the reaction, making the free energy of activation lower and the reaction faster Of course, the enzyme must find each of the substrates and organize them at the active site this is entropically unfavorable too However, the price paid for organizing the substrates can be taken out of the binding free energy (In English, the last sentence means that organizing the substrates at the active site makes the substrates bind to the enzyme less tightly than they would if they didn t have to become organized This is not a big deal since we can just increase the concentration of the substrate to what is necessary to make it bind) Entropy and disorder make good dinner conversation topics right up there with supply-side economics and the national debt
STRAIN AND DISTORTION
The binding of the substrate results in a distortion of the substrate (pulling or pushing on a bond) in a way that makes the chemical reaction easier In this model, the binding of the substrate to the enzyme strains specific chemical bonds, making the subsequent chemical reaction easier If a bond has to be broken, the enzyme grabs onto both sides of the bond and pulls If a bond has to be formed, the enzyme grabs onto both sides and pushes By this model, the enzyme must be designed to apply the strain in the right direction the direction that will help convert the reactant to the transition state (Fig 7-5)
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