BIO 1406/07 BK/LAB/CODE PREPACK
12th Edition
ISBN: 9781265538590
Author: Raven
Publisher: MCG
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Chapter 6, Problem 1S
Examine the graph showing the
a. Describe what is happening to the enzyme at around 40°C.
b. Explain why the line touches the x-axis at approximately 20°C and 45°C.
c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.
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Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the
statements that are true.
Without
enzyme
With
enzyme
A+B
Time
AB
O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction
O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the
uncatalyzed reaction
O c. The enzyme stabilizes the transition state for the reaction
Od. The reaction is exergonic
е.
The reaction is now spontaneous due to the addition of enzyme
Released Energy
Consider the following data set of enzymes A, B C and D which catalyze the same
reaction.
Enzyme A km = 5mM Vmax = 225MM/sec
Enzyme B km = 50mM Vmax = 430mM/sec
Enzyme C km = 15mM Vmax = 235mM/sec
%3D
Enzyme D km
12mM Vmax = 533mM/sec
When concentrations of substrate are very low, which is the enzyme that is
producing most product?
MacBook Air
DO
F5
S0
# 12
F4
F3
%
Sketch and label a plot showing the enzyme's initial velocity relative to pH
over the pH range 4 - 9 for the enzyme-catalyzed reaction under these two
conditions:
A. The substrate concentration is very, very high.
B. The substrate concentration is less than the enzyme's Km.
Chapter 6 Solutions
BIO 1406/07 BK/LAB/CODE PREPACK
Ch. 6.1 - Prob. 1LOCh. 6.1 - Prob. 2LOCh. 6.1 - Describe the nature of redox reactions.Ch. 6.2 - Explain the laws of thermodynamics.Ch. 6.2 - Prob. 2LOCh. 6.2 - Contrast the course of a reaction with and without...Ch. 6.3 - Describe the role of ATP in short-term energy...Ch. 6.3 - Prob. 2LOCh. 6.4 - Discuss the specificity of enzymes.Ch. 6.4 - Explain how enzymes bind to their substrates.
Ch. 6.4 - Prob. 3LOCh. 6.5 - Prob. 1LOCh. 6.5 - Prob. 2LOCh. 6.5 - Prob. 3LOCh. 6 - Prob. 1DACh. 6 - A covalent bond between two atoms represents what...Ch. 6 - During a redox reaction the molecule that gains an...Ch. 6 - Prob. 3UCh. 6 - A spontaneous reaction is one in which a. the...Ch. 6 - Prob. 5UCh. 6 - Which of the following is NOT a properly of a...Ch. 6 - Where is the energy stored in a molecule of ATP?...Ch. 6 - Prob. 1ACh. 6 - Which of the following statements is NOT true...Ch. 6 - Prob. 3ACh. 6 - Prob. 4ACh. 6 - Enzymes have similar responses to both changes in...Ch. 6 - Prob. 6ACh. 6 - Examine the graph showing the rate of reaction...Ch. 6 - Phosphofructokinase functions to add a phosphate...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Consider these three sketches: B A HHHH A A Which sketches represent the action of an enzyme? Check none of them if none of them do. And finally, for that same sketch, what is C? B |HH| For that same sketch, what is B? Again your answer should be a word or very short phrase. A B If you said at least one sketch represents the action of an enzyme, for the first sketch that does, what is A? Your answer should be a word or very short (two- or three-word) phrase. 3000|| 3 3 O (none of them) 0 0 Xarrow_forwardWhich of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pHarrow_forwardPlease handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.arrow_forward
- Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.arrow_forwardWhich of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workarrow_forwardHow would the Hill equation reveal allosteric regulation of any enzyme? Select one: а. A linear relationship between log[Y/[1- Y]] and log[S] with positive slope. b. A change in the log[Y/[1- Y]] vs. log[S] slope over a range of log[S]. c. A linear relationship between log[Y/[1- Y]] and log[S] with a negative slope. d. A constant (flat) region in the graph of log[S] vs log[Y/[1- Y]] e. None of these.arrow_forward
- a. Which unknown sample is the negative control? And Which unknown sample is the positive control? b. The experiment she conducted aimed to determine the action of what enzyme?arrow_forwardConsider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?arrow_forwardA newly developed drug is suspected to act by inhibiting its enzymatic target. To test this, the rates of reaction in the presence and absence of the new drug were determined. The results of these experiments have been plotted as a double reciprocal plot shown in figure 1 below. Using this figure, calculate the values of Vmax and Km for the enzyme in the presence and absence of the drug. Based on the figure and your answer, what type of inhibition is the new drug displaying? Briefly explain how this type of inhibition exerts its action on an enzyme.arrow_forward
- The figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?arrow_forwardEnzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligasearrow_forwardConsider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pesarrow_forward
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