The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained. Concept introduction: Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

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Answer 1

Question

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

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Students have asked these similar questions

The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help

To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?

To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!

Answer 2

Question

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

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Answer 3

Question

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

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Answer 4

Question

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

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Answer 5

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

Answer 6

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

Answer 7

Chapter 14, Problem 1P

Interpretation Introduction

Interpretation:

The reason for the generation of active enzymes due to mutation of serine or threonine residues to form aspartate needs to be explained.

Concept introduction:

Protein kinase is a type of kinase enzyme that modifies the biological activities of proteins by phosphorylating a specific kind of amino acid by using ATP as a source of phosphate.

Answer 8

Expert Solution & Answer

Answer to Problem 1P

The mutation of serine or threonine substantially increases the ubiquitin-conjugating activities. Hence, it helps in the generation of active enzymes.

Answer 9

Expert Solution & Answer

Answer 10

Expert Solution & Answer

Answer 11

Explanation of Solution

In order to activate the protein kinases, phosphorylation can be done either on serine or on threonine residues because both of these are neutral residues. On getting phosphorylated, these get negatively charged. If serine and threonine is substituted by glutamate, then negatively charged glutamate is preferred more than the negatively charged phosphoserine or phosphothreonine to alter the tertiary structure of protein kinase into the active state.

Answer 12

Conclusion

Thus, by increasing the ubiquitin-conjugating activity substantially, mutation of serine or threonine leads to the generation of active enzymes.

Answer 13

Ch. 14 - Prob. 1P Ch. 14 - Prob. 2P Ch. 14 - Prob. 3P Ch. 14 - Prob. 4P Ch. 14 - Prob. 5P Ch. 14 - Prob. 6P Ch. 14 - Prob. 7P Ch. 14 - Prob. 8P Ch. 14 - Prob. 9P Ch. 14 - Prob. 10P

Answer to Problem 1P

Explanation of Solution

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Chapter 14 Solutions