Homework Answers
Serine protease have a catalytic triad of serine , histidine and aspartic acid, where as aspartic protease have two aspartic acid in active site.
In serin protease there is a covalent intermediate, where as aspartic protease utilizes the direct nucleophilic attack by water.
A similarly between both mechanisms is that they go through a tetrahedral intermediate intermediate.
Add Answer to:
Anyone can help me with it?
Compare and contrast serine proteases and aspartic proteases. Not all...
Compare and contrast serine proteases and aspartic proteases. Not all answers will be used. Question 3...
Compare and contrast serine proteases and aspartic proteases.
Not all answers will be used.
Question 3 of 5 Map Serine protease Both Aspartic protease direct electrophilic covalent tetrahedral trigonal planar catalytic triad of serine, four aspartic acids catalytic triad of serine, direct nucleophilic two aspartic acids intermediate attack by water intermediate intermediate leucine, and valine attack by waterin active site in active site histidine, and aspartic acid O Previous ⓧ Give Up & View Solution O Check Answer 0 Next...
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...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All the protease mechanisms we discussed in class involved formation of a covalent acyl enzyme intermediate. O Alinear polymer of glucose joined by a(1,6) linkages. True False O A polymer of glucose joined by a(1,4) linkages with a(1,6) linkages every 5-10 residues. Question 4 (1 point) O A polymer of glucose joined by B(1,4) linkages with a(1,6) linkages every 5-10 residues. In the mechanism of...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All the protease mechanisms we discussed in class involved formation of a covalent acyl enzyme intermediate. O Alinear polymer of glucose joined by a(1,6) linkages. True False O A polymer of glucose joined by a(1,4) linkages with a(1,6) linkages every 5-10 residues. Question 4 (1 point) O A polymer of glucose joined by B(1,4) linkages with a(1,6) linkages every 5-10 residues. In the mechanism of...
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...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without...
Under typical conditions, many essential biochemical reactions
proceed so slowly that life could not exist without the presence of
enzymes. Enzymes increase reaction rates through a wide variety of
mechanisms. These mechanisms generally utilize the following
strategies: improving the nucleophiles and electrophiles present in
the catalytic R groups or substrates; stabilizing the extra
electron density of the leaving group; and stabilizing transition
states. Proteases are enzymes that break down proteins by
hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
biochemistry class homework Under typical conditions, many essential biochemical reactions proceed so slowly that life could...
biochemistry class
homework
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a variety of mechanisms. These mechanisms generally utilize strategies such as improving the nucleophiles and electrophiles present in the catalytic R groups or substrates, stabilizing the extra electron density of the leaving group, and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease...
Compare and contrast serine proteases and aspartic proteases.
Not all answers will be used.
Question 3 of 5 Map Serine protease Both Aspartic protease direct electrophilic covalent tetrahedral trigonal planar catalytic triad of serine, four aspartic acids catalytic triad of serine, direct nucleophilic two aspartic acids intermediate attack by water intermediate intermediate leucine, and valine attack by waterin active site in active site histidine, and aspartic acid O Previous ⓧ Give Up & View Solution O Check Answer 0 Next...
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...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All the protease mechanisms we discussed in class involved formation of a covalent acyl enzyme intermediate. O Alinear polymer of glucose joined by a(1,6) linkages. True False O A polymer of glucose joined by a(1,4) linkages with a(1,6) linkages every 5-10 residues. Question 4 (1 point) O A polymer of glucose joined by B(1,4) linkages with a(1,6) linkages every 5-10 residues. In the mechanism of...
Question 1 (1 point) Which of the following best describes glycogen? Question 3 (1 point) All the protease mechanisms we discussed in class involved formation of a covalent acyl enzyme intermediate. O Alinear polymer of glucose joined by a(1,6) linkages. True False O A polymer of glucose joined by a(1,4) linkages with a(1,6) linkages every 5-10 residues. Question 4 (1 point) O A polymer of glucose joined by B(1,4) linkages with a(1,6) linkages every 5-10 residues. In the mechanism of...
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...
Under typical conditions, many essential biochemical reactions
proceed so slowly that life could not exist without the presence of
enzymes. Enzymes increase reaction rates through a wide variety of
mechanisms. These mechanisms generally utilize the following
strategies: improving the nucleophiles and electrophiles present in
the catalytic R groups or substrates; stabilizing the extra
electron density of the leaving group; and stabilizing transition
states. Proteases are enzymes that break down proteins by
hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
biochemistry class
homework
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a variety of mechanisms. These mechanisms generally utilize strategies such as improving the nucleophiles and electrophiles present in the catalytic R groups or substrates, stabilizing the extra electron density of the leaving group, and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease...
Most questions answered within 3 hours.
-
Which of the following does NOT add to US GDP? A. Saudi Arabia
buys fighter jets...
asked 1 hour ago -
2. Describe market equilibrium in terms of the following
characteristics
d.
How supply and demand interactions...
asked 1 hour ago -
1a. Create a class named Computer
- Separate declaration from implementation (i.e. Header and CPP
files)...
asked 1 hour ago -
A medical researcher
believes that a drug changes the body's temperature. Seven test
subjects are randomly...
asked 1 hour ago -
A call option on Project Cash Flow Consulting Inc.'s stock (PCF)
has a market price of...
asked 1 hour ago -
A study on the latest fad diet claimed that the amounts of
weight lost by all...
asked 2 hours ago -
give examples of how gene expression is inherited to the next
generation?
asked 2 hours ago -
If a project has _________ IRR(s), we should __________ . Assume
this project is competing with...
asked 2 hours ago -
In the figure, a sound of wavelength 0.700 m is emitted
isotropically by point source S....
asked 2 hours ago -
1) Stock X has a beta of 1.6. If the risk free rate is 3.4
percent...
asked 2 hours ago -
Gallium is produced by the electrolysis of a solution obtained
by dissolving gallium oxide in concentrated...
asked 2 hours ago -
A small company that manufactures juggling equipment makes 19
different types of clubs. The company wants...
asked 2 hours ago