The features of an enzyme structure that makes it specific for a specific substrate. Introduction: Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

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Answer 1

Question

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

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Students have asked these similar questions

UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?

A carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.

Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.

Answer 2

Question

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

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Answer 3

Question

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

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Answer 4

Question

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

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Answer 5

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

Answer 6

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

Answer 7

Chapter 6, Problem 1Q

Summary Introduction

To review:

The features of an enzyme structure that makes it specific for a specific substrate.

Introduction:

Enzymes are chemically proteins in their folded tertiary structure and contain specific active sites. Hexokinase belongs to a class of enzyme that catalyzes the adenosine triphosphate(ATP)dependent phosphorylation of certain hexoses (six carbon sugars). They only bind to sugar thatis in D-form. The interaction between enzyme and substrate is highly specific.

Answer 8

Expert Solution & Answer

Explanation of Solution

Every enzyme has an active site, which is specific for a specific substrate. This can be illustrated by the lock and key model. A particular key can open a particular lock, likewise a particular enzyme can catalyze a particular substrate. This is the most important feature of enzyme specificity. Incase of hexokinase, they have an active site that is specific for only D-form of hexose sugars. Both substrate and enzyme have complementary structures, which facilitate their interaction.

Specificity of the enzyme depends upon the interaction of active site amino acids with the substrate. Some enzymes requirenonprotein components called cofactors for their activity. The cofactors may be ions, such as Mg2+ or Zn2+. Thesemay also be complex organic molecules called coenzymes. Cofactors and coenzymes also enhance the functioning of specific enzymes by making the active site more favorable for binding of substrates.

Answer 9

Expert Solution & Answer

Answer 10

Expert Solution & Answer

Answer 11

Conclusion

Thus, it can be concluded that the enzyme has an active sit, ehich has the structure complementary to the specific substrate. This is like a lock and key. There are cofactors and coenzymes that are also responsible for the specificity of the enzyme.

Answer 12

Ch. 6 - Prob. 1Q Ch. 6 - Prob. 2Q Ch. 6 - Prob. 3Q Ch. 6 - Prob. 4Q Ch. 6 - Prob. 5Q Ch. 6 - Prob. 6Q Ch. 6 - Prob. 7Q Ch. 6 - Prob. 8Q Ch. 6 - Prob. 9Q Ch. 6 - Prob. 1RQ

Explanation of Solution

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