SmartUnicorn
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So I got taught that a binding agent would change the tertiary structure meaning the active site is no longer complimentary, therefore no more enzymatic reactions can take place?

Q: a sugar called lyxose increases rate of reaction. how does it lower the activation energy?

I don’t understand how it would speed up the reaction?
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ab_112
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I think that lyxose might be an enzyme. Since enzymes work by lowering the activation energy by providing an alternative energy pathway, where the activation energy is lower, for particles to react. This way particles that don't have enough energy also react and so more successful collisions and the reaction happens faster if that makes sense.

https://www.physicsandmathstutor.com/biology-revision/
Physic and Maths Tutor have summary notes you can look up and it usually helps. Also, they have specific exam boards as well and they have questions as well. Should check it out, it really helps me!
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sprucicles10101
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Hey I don't know if you already got help with this but:

The sugar will bind to the enzyme's allosteric site causing the bonds in the tertiary structure to slightly change, per the induced fit model, so that the active site changes shape to become a better fit for the substrate, which can bind (forming an enzyme-substrate complex) thereby distorting the bonds in the substrate and reducing the activation energy.

Its somewhat related to co-enzymes which come up in photosynthesis and respiration

Hope this helped
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SmartUnicorn
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(Original post by sprucicles10101)
Hey I don't know if you already got help with this but:

The sugar will bind to the enzyme's allosteric site causing the bonds in the tertiary structure to slightly change, per the induced fit model, so that the active site changes shape to become a better fit for the substrate, which can bind (forming an enzyme-substrate complex) thereby distorting the bonds in the substrate and reducing the activation energy.

Its somewhat related to co-enzymes which come up in photosynthesis and respiration

Hope this helped
So does a sugar changing the tertiary structure mean that the enzyme will fit the substrate better? Is it only a sugar that does this? Thankyou!
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sprucicles10101
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(Original post by SmartUnicorn)
So does a sugar changing the tertiary structure mean that the enzyme will fit the substrate better? Is it only a sugar that does this? Thankyou!
Aha no problem, so you know how normally a non-competitive inhibitor would break bonds in the tertiary structure of the active site meaning it is no longer complementary to the substrate. The sugar is responsible for the opposite. The induced fit model says that the active site isnt completely complementary to the substrate and that when it forms a enzyme-substrate complex, the active site will form around the substrate making it more complementary. So the sugar will change the bonds in the tertiary sugar so that the active site becomes more complementary to the substrate. So when the enzyme-substrate complex forms, the bonds in the substrate can be weakened/distorted so that it can be broken down quicker.
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