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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.

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How does an an enzymes active site relate to its substrate?

The active site is the specific region of the enzyme which combines with the substrate. The binding of the substrate to the enzyme causes changes in the distribution of electrons in the chemical bonds of the substrate and ultimately causes the reactions that lead to the formation of products.


When the substrates are bound to the enzyme it is called the?

An active site. Sometimes the active site can be disabled from inhibitors.


What are the names of the enzyme?

Hydrolases - Hydrolysis of a substrate - digestive enzyme isomerases - change of the molecular form of the substrate - famerase


What is a substrate that fits into an area of an enzyme?

A substrate is a molecule that fits into the active site of an enzyme. The active site is a specific region of the enzyme where the substrate binds, allowing the enzyme to catalyze a specific chemical reaction.


What is the place where the substrate attaches to the enzyme?

The active site is where the substrate binds to the enzyme. It is a region on the enzyme where the chemical reaction takes place. The active site is specific to the substrate molecule, allowing for precise catalysis to occur.


The binding together of an enzyme and a substrate forms a what?

enzyme-substrate complex


Why catalase only works with one substrate?

Catalase is an enzyme that specifically acts on hydrogen peroxide (H2O2) as its substrate. The enzyme's active site is complementary to the structure of H2O2, allowing it to effectively bind and break down the substrate into water and oxygen. This specificity is a key feature of enzymatic reactions, ensuring efficient and selective catalysis.


What to enzymes do in an enzyme-substrate?

in an enzyme-substrate complex, the enzyme acts on the substrate .


Where do non-competitive inhibitors bind in relation to the enzyme's active site?

Non-competitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing the substrate from binding effectively.


What is the difference between the lock and key model versus the induced fit model of the enzyme substrate complex?

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.


What is it called when and enzyme and substrate come together?

When an enzyme and substrate come together, it is called the enzyme-substrate complex. This complex is a temporary intermediate state in which the enzyme binds to the substrate to catalyze a chemical reaction.


Are enzyme natural sites complementary to their substrates?

Yes, enzyme active sites are naturally complementary to their substrates in terms of shape, size, and chemical properties. This complementarity facilitates specific binding, allowing enzymes to catalyze reactions effectively. The structural compatibility between the enzyme and substrate enhances the likelihood of interaction, ultimately leading to the formation of the enzyme-substrate complex. This specificity is crucial for the enzyme's biological function.