Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- 1. A substrate is converted to product using an enzyme that follows the mechanism below when an inhibitor (1) and an activator (A) are both present in the reaction mixture. ES (2)→→ E + P E+S (1) E +1 < (3) → EI E+A← (4)→ EA {the inhibitor and activator do not bind simultaneously} EI + S EA+S (5) → EIS -(6)→ EI + P (7)→ EAS-(8)→ EA + P with reaction rate constants of k₁ and k.₁ (and so on) for each of the reactions: A. Although this mechanism does not match exactly any of the inhibitor mechanisms discussed in class, which type of inhibitor is this most like (competitive, uncompetitive or non-competitive)? B. Write the enzyme balance equation. C. Write the total rate of product, P, formation based on the kinetic rate constants and concentrations of intermediate species. D. Write each of the equations that result from applying the rapid equilibrium and quasi steady state assumptions. E. Knowing that I is an inhibitor and A is an activator, discuss the relative values of k₂, k6 and kg.arrow_forward11. (ME.23) Given the pathway below, steps catalyzed by enzymes, are good candidates for regulation and compound negatively regulate enzyme 5. A. All steps with -AG; compound H B. Steps catalyzed by enzymes 2 and 5 only; compound C C. Steps catalyzed by enzymes 4 and 5 only; compound H D. Steps catalyzed by enzymes 2, 4, 5, 6 & 8; compound C E. Steps catalyzed by enzymes 2, 4, 5, & 8; compound H A is a good candidate to AG +0.1 enz7 AG AG AG H AG AG +1.1 -23.3 -0.7 -1.4 -16.7 enz1 enz2 enz3 AG enz4 enz5 -arrow_forwardHydrogen peroxide (H2O2) is a toxic chemical (waste product) that is produced when our bodies break down amino acids and complete other important metabolic reactions. Catalase is an enzyme found in our livers that is responsible for the decomposition (break down) of hydrogen peroxide into the harmless compounds of water and oxygen. Due to the enzyme's action, the cells in our bodies are able to rid themselves of the harmful H2O2 waste product. Without the catalase enzyme, many of our cells would be damaged by the increased amount of H2O2. When the enzyme is working, oxygen gas bubbles will be released. The chemical reaction that occurs is the following: catalase 2H2O2 → 2H,O + O2 Students in biology class performed an experiment to test the activity of catalase at different pH levels. The diagram below represents the students’ results. I II III IV V bubbles of. oxygen gas piece of liver containing catalase Strongly Acidic Solution Weakly Acidic Solution Strongly Basic Solution Weakly…arrow_forward
- 4) Enzyme 1 and 2 catalyze the same reaction. Both enzymes have the same Km, but Enzyme 1 has a higher Vmax. A. Sketch out what both enzymes look like in a lineweaver burk plot. B. You test an inhibitor (compound A) on both enzymes. In Enzyme 1 The apparent Km increases, in enzyme 2 both the Km and Vmax decrease. What does this suggest about what kind of inhibitor compound A is in each enzyme?arrow_forward6) What is the approximate temperature (in both F° and C°) for enzyme activity in the human body?arrow_forward7. Fill in the blank with the correct terms. Phosphorylation and dephosphorylation are what type of enzyme regulation methods? а. Type of non-permanent enzyme inhibition that does not directly interfere with the enzymes active site. Class of enzyme that hydrolyzes esters, amides, and phosphoesters. C. Name of an enzyme that would catalyze the removal of hydrogen from alcohols (product would be an aldehyde). d. Rank the energy bearing phosphate compounds AMP, ATP, and ADP from the citric acid cycle in order of highest energy to lowest. b. e.arrow_forward
- 32. Which of the following is true? A. An exergonic reaction, energy is released and the delta G is positive B. An exergonic reaction, energy is stored and the delta G is negative C. An exergonic reaction, energy is released and the delta G is negative D. An exergonic reaction, energy is stored and the delta G is positivearrow_forward5. Some enzymes can catalyze substrate reactions which result in the production of H* ions. If the batch reactor is not sufficiently buffered, this can lead to a change in pH. Because pH is an important factor in optimizing enzyme activity, the reaction velocity v can be altered during the reaction by the appearance of H* as a product. On a single graph, sketch a qualitative velocity profile (velocity vs. time) for the enzymatic breakdown of the substrate Auburn by the enzyme, WarEaglease for two conditions: A. An unbuffered solution that starts at pH 9. B. A well-buffered pH 9 solution. C. A well-buffered pH 7 solution. Relative Activity (%) 100 90 80 70 60 50 40 30 20 10 0 Activity of WarEagle ase 2 3 4 7 8 9 10 11 12 13 14 PH The substrate, Auburn, is a weak base, and the reaction is carried out in a batch reactor. Assume a high substrate concentration, so depletion of [S] does not cause the reaction to slow during the experiment. The relative activity of WarEaglease as a function…arrow_forwardA. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?arrow_forward
- Which of the following is not a mechanism that enzymes use to lower the activation energy of a reaction?arrow_forward2. (Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? R CO₂H A R SCOA B R Rarrow_forwardMany enzyme mechanisms involve transferring protons. Sidechains of an enzyme can act as catalytic acids or catalytic bases in this process. The figure below shows a step in the reaction by the enzyme triose phosphate isomerase. Glu165 group. -OH Would a catalytic acid gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic acid? co CH,OPO, 2- Activity remaining (%) Would a catalytic base gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic base? 100 Curve I 8 Glu¹65 9 Below are two pH rate profiles showing the percent activity as a function of pH. Answer the questions below about how these curves relate to the mechanism of triose phosphate isomerase. Remember what fraction of a titratable group is unprotonated at the pka. 10 OH In this reaction a carbonyl is converted into an enol intermediate. Circle the enol 100 Activity remaining (%) H Curve 2 CIOH CIOH CH₂OPO,²- 8 9 N N 10 7 pH PH i) Which of these curves shows the pH rate…arrow_forward
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