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An enzyme's active site will bind with only a specific substrate. Any other kind of substrate will be rejected by the active site.

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What would be unlikely to contribute to the substrate specificity of an enzyme?

The size of the enzyme's active site would not contribute significantly to substrate specificity. Substrate specificity is typically determined by the shape, charge, and chemical properties of the active site that can properly bind to the substrate.


What causes enzyme specificity?

Enzyme specificity is mainly determined by the active site structure and the interactions between the enzyme and its substrate. The shape, charge, and chemical properties of the active site are crucial in determining which substrates can bind to the enzyme and undergo a catalyzed reaction. Additionally, enzymes undergo conformational changes upon substrate binding to further enhance specificity.


Explain the difference between substrate and active site?

The substrate is the molecule that binds to the active site of an enzyme. The active site is a region on the enzyme where the substrate binds and undergoes a chemical reaction. The specificity of the active site allows only certain substrates to bind and react with the enzyme.


Why does enzymes only work on one substance?

Enzymes have a specific shape that is complementary to the shape of their target substrate. This specificity allows enzymes to bind to only certain substrates, aiding in catalyzing specific chemical reactions. Furthermore, the active site of the enzyme is designed to interact with specific functional groups on the substrate, enhancing its specificity.


Enzyme is limited in its ability to join with a particular molecule by the what?

Enzymes are limited in their ability to bind with a particular molecule by their specificity. Enzymes have specific active sites that only bind to certain substrates based on their shape and chemical properties. This specificity allows enzymes to catalyze specific reactions in biological systems.

Related Questions

Does the shape of an enzyme protein determine specificity?

Shape of an enzyme specifically shape of its active site determines enzyme specificity .


What would be unlikely to contribute to the substrate specificity of an enzyme?

The size of the enzyme's active site would not contribute significantly to substrate specificity. Substrate specificity is typically determined by the shape, charge, and chemical properties of the active site that can properly bind to the substrate.


What causes enzyme specificity?

Enzyme specificity is mainly determined by the active site structure and the interactions between the enzyme and its substrate. The shape, charge, and chemical properties of the active site are crucial in determining which substrates can bind to the enzyme and undergo a catalyzed reaction. Additionally, enzymes undergo conformational changes upon substrate binding to further enhance specificity.


Explain the difference between substrate and active site?

The substrate is the molecule that binds to the active site of an enzyme. The active site is a region on the enzyme where the substrate binds and undergoes a chemical reaction. The specificity of the active site allows only certain substrates to bind and react with the enzyme.


What is the definition of enzyme specificity?

each enzyme has a specific substrate to which it binds through a definite active site and any other enzyme can not bind to it


Is Enzyme structure is important because the enzymes shape allows only certain substrates to bind to the enzyme?

Yes, the stucture of an enzyme's active site (which binds to substrates) and other areas that bind to cofactores are important. Only certain substrates will link to it depending on the shape, eletrostatic interactions and hydrophobicity of an active site.


How is protein structure involved in enzyme specificity?

Protein structure plays a key role in enzyme specificity by determining the shape and active site of the enzyme. The unique 3D structure of an enzyme's active site allows it to bind specific substrates with complementary shapes, leading to catalysis of specific chemical reactions. Any changes in the enzyme's structure can affect its ability to recognize and bind to its substrate, thereby impacting its specificity.


What are the deep folds in an enzyme called?

The deep folds in an enzyme are called active sites. These are specific regions where substrate molecules bind and chemical reactions take place. Active sites are crucial for enzyme function and specificity.


What happen to the active site when the enzyme denatures?

The action going on that site will slow down.


What happens if enzymes loose their specificityAsk us anything?

They can't catalyse reactions. The specificity of the active site of the enzyme is crucial: without it, the enzyme won't fit with he desired substrate, hence there won't be any reaction. Losing this specificity is due to a conformational change at the active site, andis known as denaturisation.


How might a change of one amino acid at a site distant from the active site of an enzyme alter an enzyme's substrate specificity?

A change of one amino acid at a site distant from the active site of an enzyme can alter the enzyme's substrate specificity by affecting the overall conformation or stability of the enzyme. This alteration can influence how the enzyme binds to its substrate, either by modifying the shape of the active site or by impacting the enzyme's interactions with other molecules. Additionally, such a change might affect the dynamics of the enzyme, potentially enhancing or diminishing its ability to recognize particular substrates. Hence, even distant amino acid substitutions can have significant functional consequences on enzyme activity.


Is an enzyme specific in terms of which substrates it can bind?

Yes, enzymes are specific in terms of the substrates they can bind. Each enzyme has an active site that can only accommodate certain substrates based on their shape and chemical properties. This specificity allows enzymes to catalyze specific biochemical reactions.