29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ Asp 102 H₂C CH₂ New N-terminus of cleaved polypeptide chain His 57 Ser (195) C=0 CH₂

29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ Asp 102 H₂C CH₂ New N-terminus of cleaved polypeptide chain His 57 Ser (195) C=0 CH₂

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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2. What is the chemical formula of analdosecarbohydrate molecule? 3. How many H2O molecules and C molecules is there in analdose? 4.What enzyme is missing in people who are lactose intolerant? What is the functionof this enzyme and why does it make people feel sick?
Why do you think both enzymes tested have the exact same optimal working temperature (i.e. temperature they work best at)?
The substrate dissociation constant, Ks, is k-1/k1. What do large values of this constant mean? That the formation of product will be fast Strong binding between enzyme and substrate that the reaction is unimolecular Weak binding between enzyme and substrate
help with question 5 please
The following graph shows the activity versus pH curve for pepsin, an enzyme that breaks down proteins into smaller peptides. Estimate its optimum pH. Maximum activity No activity pH 0 pH 3.8 pH 2 O pH4 Pepsin 01 2 3 pH 4 5
Match each enzyme class to the type of reactions catalyzed. Enzyme Class Type of Reactions Catalyzed reactions involving the transfer of a functional group from one molecule to another energetically unfavorable reactions that require ATP to form new bonds oxidation-reduction reactions reactions that eliminate or form a double bond hydrolysis reactions isomerization reactions Answer Bank hydrolase lyase ligase oxidoreductase isomerase transferase
An enzyme has an optimal pH of 7.1 and an optimal temperature at 37° C. Which statement describes a reaction catalyzed by this particular enzyme at a constant temperature of 20° C? the reaction will slow down and then increase as the temperature increases O there is no effect O the reaction will be slower than if it ran at 37° C O the enzyme will provide an alternate active site so the reaction can proceed the enzyme will be denatured
Proteins are thermodynamically unstable molecules since the Delta G of hydrolysis is quite negative. However, most proteins are not degraded unless they come into contact with proteases in cells. What is the reasoning for this paradox? The reaction is endergonic and will not proceed without energy. There is very little water inside cells to react with protein molecules. The free energy change doesn't reveal anything about the rate of the reaction. The concentration of proteins are low which allows them to be more stable.
What impact on k1 and k-1 would be when a mutation in the enzyme (E) makes the interaction between E and its substrate (S) stronger? a. k1 increase and k-1 decrease b. k1 decrease and k-1 decrease c. k1 decrease and k-1 increase d.
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9. To what main enzyme class do the enzymes that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO H H₂N-C-CN-C-coo + H₂0- II HR₂ 1 R₁ This bond is cleaved H H₂N-C-Coo R₂ H₂N H 1 R₁ -COOⒸ