The chymotrypsin catalytic triad contains one Histidine and one Serine residue. Explain, in some detail and...
The chymotrypsin catalytic triad contains one Histidine and one Serine residue. Explain, in some detail and in chemical terms, how an
a) a Histidine to Alanine mutation, and
b) a Serine to Cysteine mutation
in the chymotrypsin catalytic triad might affect catalytic activity of this enzyme.
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The chymotrypsin catalytic triad contains one Histidine and one
Serine residue. Explain, in some detail and...
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the...
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids serine, histidine, and aspartate the amino acids cysteine, histidine, and aspartate the enzyme-cofactor-substrate complex the amino acids serine, histidine, and glutamate
A bioinformatics study revealed that the enzymes called vasoinhibins have a Cys–His–Ser catalytic triad. These enzymes...
A bioinformatics study revealed that the enzymes called vasoinhibins have a Cys–His–Ser catalytic triad. These enzymes regulate angiogenesis (the formation of new blood vessels) and are thus potential drug targets for cancer treatment. If the cysteine residue serves as the nucleophile, what are the possible roles of histidine and serine in enzyme catalysis?
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser...
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
1. ASP has an important role in hydrogen bonding with the His residue in the catalytic...
1. ASP has an important role in hydrogen bonding with the His residue in the catalytic triad of chymotrypsin. ASP and GLU have very similar properties as amino acids. Yet, mutation of ASP to GLU in the traid results in a 10^5 fold decrease in enzyme activity. Why do you think this could be the case?
Based on what we've learned about the enzyme chymotrypsin: a) Explain the general role of each...
Based on what we've learned about the enzyme chymotrypsin: a) Explain the general role of each catalytic residue in the chymotrypsin catalytic triad. b) Describe the catalytic strategy or strategies used by chymotrypsin. c) Identify the class of enzymes chymotrypsin belongs to. 7. At a molecular level, how do carbon dioxide and hydrogen ions regulate oxygen binding to hemoglobin?
(5) Describe the chemical properties of zinc that are relevant to its catalytic role in hydrolytic...
(5) Describe the chemical properties of zinc that are relevant to its catalytic role in hydrolytic enzymes (6) The protein liver alcohol dehydrogenase (LADH) contains two zinc sites. The first has 4 cysteine ligands and the second has 2 histidine, 2 cysteine and one water ligand. Explain why there is a difference and how the difference relate to the function of LADH?
(5) Describe the chemical properties of zinc that are relevant to its catalytic role in hydrolytic enzymes (6)...
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to...
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to be important in stabilizing the transition state of the bound substrate. a) Sketch a graph showing the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pH-activity profile of the enzyme. Provide the biochemical basis for your graph. b) Identify one of the two substrates involved in the reaction catalyzed by ATCase and the enzyme class for ATCase....
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate conformation. Also explain how contribute to enzyme action. In other words, how do these weak intera enzyme and the transition state lower the activation energy?) of making the enzyme active site complementary to the transition nation. Also explain how multiple weak interactions words, how do these weak interactions between the 25. 1/F. The pk's of titratable groups of amino acids remain constant irrespective of...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and ...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids serine, histidine, and aspartate the amino acids cysteine, histidine, and aspartate the enzyme-cofactor-substrate complex the amino acids serine, histidine, and glutamate
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
Based on what we've learned about the enzyme chymotrypsin: a) Explain the general role of each catalytic residue in the chymotrypsin catalytic triad. b) Describe the catalytic strategy or strategies used by chymotrypsin. c) Identify the class of enzymes chymotrypsin belongs to. 7. At a molecular level, how do carbon dioxide and hydrogen ions regulate oxygen binding to hemoglobin?
(5) Describe the chemical properties of zinc that are relevant to its catalytic role in hydrolytic enzymes (6) The protein liver alcohol dehydrogenase (LADH) contains two zinc sites. The first has 4 cysteine ligands and the second has 2 histidine, 2 cysteine and one water ligand. Explain why there is a difference and how the difference relate to the function of LADH?
(5) Describe the chemical properties of zinc that are relevant to its catalytic role in hydrolytic enzymes (6)...
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to be important in stabilizing the transition state of the bound substrate. a) Sketch a graph showing the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pH-activity profile of the enzyme. Provide the biochemical basis for your graph. b) Identify one of the two substrates involved in the reaction catalyzed by ATCase and the enzyme class for ATCase....
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate conformation. Also explain how contribute to enzyme action. In other words, how do these weak intera enzyme and the transition state lower the activation energy?) of making the enzyme active site complementary to the transition nation. Also explain how multiple weak interactions words, how do these weak interactions between the 25. 1/F. The pk's of titratable groups of amino acids remain constant irrespective of...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
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