Compare and contrast serine proteases and aspartic proteases. Not all answers will be used.
Compare and contrast serine proteases and aspartic proteases. Not all answers will be used. Question 3...
Anyone can help me with it? Compare and contrast serine proteases and aspartic proteases. Not all answers will be used. Serine protease Both Aspartic protease catalytic triad of serine, histidine, and aspartic acid two aspartic acids in active site tetrahedral intermediate covalent intermediate direct nucleophilic attack by water Answer Bank trigonal planar intermediate four aspartic acids in active site direct electrophilic attack by water catalytic triad of serine, leucine, and valine
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...
My answers are: Question 1: False Question 4: proton transfer with a pK close to 4 Question 5: the active site contains an aspartic acid and glutamic acid, both of which must be deprotonated Question 8: 2 histidine residues with somewhat different pKa values act as acids and bases during catalysis Can someone please check my answers? Question 1 (1 point) Cellulose and glycogen are both structural polysaccharides True False Question 4 (1 point) _ in the A pH versus...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active site of the enzyme chymotrypsin. what are the identities of amino acids x and Y and what is this particular type of spatial arrangement of amino acids called? Alkoxide on X ? B. from the strucutres shown below, identify the two that represent the first and the second tetrahedral intermediates in the chymotrypsin catalyzed reaction. what type of attack and...
Question 6 (1 point) in the A pH versus rate curve with an inflection point at pH-4 suggests the involvement of an catalytic step Question 8 (1 point) Cellulose and glycogen are both structural polysaccharides proton donation that is mediated by a coenzyme True False free proton surrounded by a hydrophobic environment proton transfer with a pK close to 4 Question 9 (1 point) proton abstraction that requires a metal ion in close proximity The activity of lysozyme is greater...
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...