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.

Question

Want to see more full solutions like this?

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Students have asked these similar questions

Compare and contrast primary and secondary active transport mechanisms in terms of energy utilisation and efficiency. Provide examples of each and discuss their physiological significance in maintaining ionic balance and nutrient uptake. Rubric Understanding the key concepts (clearly and accurately explains primary and secondary active transport mechanisms, showing a deep understanding of their roles) Energy utilisation analysis ( thoroughly compares energy utilisation in primary and secondary transport with specific and relevant examples Efficiency discussion Use of examples (provides relevant and accurate examples (e.g sodium potassium pump, SGLT1) with clear links to physiological significance. Clarity and structure (presents ideas logically and cohesively with clear organisation and smooth transition between sections)

9. Which one of the compounds below is the major organic product obtained from the following reaction sequence, starting with ethyl acetoacetate? 요요. 1. NaOCH2CH3 CH3CH2OH 1. NaOH, H₂O 2. H3O+ 3. A OCH2CH3 2. ethyl acetoacetate ii A 3. H3O+ OH B C D E

7. Only one of the following ketones cannot be made via an acetoacetic ester synthesis. Which one is it? Ph کہ A B C D E

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

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

Want to see more full solutions like this?

Chapter 6 Solutions