Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 36, Problem 5TYK
Summary Introduction
Introduction: The temperature coefficient is a factor that indicates the rate of change of a reaction as a result when the temperature increases by 10ºC. The temperature coefficient is denoted by Q10. The formula for temperature coefficient is
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It takes 9.4 msec for Enzyme X to catalyse a single reaction when it is fully saturated with substrate. Calculate the Vmax of
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Time (minutes)
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a newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180 kDa and SDS-PAGE shows it to be a homodimer. 1 mg of enzyme produces a 0.05 moles of product per minute per ml. What is the turnover number of this enzyme in µmole product produced per µmole of enzyme subunit per ml?
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Chapter 36 Solutions
Study Guide for Campbell Biology
Ch. 36 - Prob. 1IQCh. 36 - a. A flaccid plant cell has a water potential of...Ch. 36 - Prob. 3IQCh. 36 - Prob. 4IQCh. 36 - Prob. 5IQCh. 36 - Prob. 6IQCh. 36 - Prob. 1SYKCh. 36 - Prob. 2SYKCh. 36 - If a plant has a phyllotaxy of alternate leaves...Ch. 36 - Prob. 2TYK
Ch. 36 - Prob. 3TYKCh. 36 - Prob. 4TYKCh. 36 - Prob. 5TYKCh. 36 - Prob. 6TYKCh. 36 - Prob. 7TYKCh. 36 - Prob. 8TYKCh. 36 - Prob. 9TYKCh. 36 - Prob. 10TYKCh. 36 - Prob. 11TYKCh. 36 - Prob. 12TYKCh. 36 - Prob. 13TYKCh. 36 - Prob. 14TYKCh. 36 - Prob. 15TYKCh. 36 - Your favorite houseplant is wilting. Which of the...Ch. 36 - Prob. 17TYKCh. 36 - Which of the following mechanisms explains the...Ch. 36 - Prob. 19TYKCh. 36 - Prob. 20TYK
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- What type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown in the graph below where the solid Ine represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhíbítion B. Noncompetitive inhíbition C. Competitive inhíbition D. Uncompetitive inhibition Potassium cyanide ia a polson which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? A. Irreveraible inhibition c. Competitive inhibition D. Uncompetitive inhibition B. Noncompetitive inhibition _10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase в. Нуdrolase c. Isomerase D. Ligase Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase…arrow_forwarda. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What kind of reaction occurred when 1 was converted to 2? d. What general kind of enzyme might you expect to perform this reaction? e. What cofactor, if any, would be required for this reaction?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_forward
- a. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What molecule a is required for this reaction to proceed? d. What molecule b is produced in addition to 2? e. What enzyme performs this reaction?arrow_forwardDefine the following terms: a. adenosine triphosphate b. redox reaction c. oxidizing agent d. reducing agent e. NADHarrow_forwardMatch each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. Lyasearrow_forward
- An enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-1arrow_forwardUrea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37°C (the optimum temperature) to 27°C? (Circle one). a. There will be no effect. b. The rate will slow down. c. The rate will double. d. The rate will triple.arrow_forwardThe Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the reaction of the reaction when the substrate concentration is 7 × 10−2 mmol/min? a. 35 mmol/min b. 50 mmol/min c. 60 mmol/min d. 70 mmol/minarrow_forward
- What is the initial rate of reaction show by the data in the graph below? A. 0.6 mmol per litre / second B. 6 mmol per litre / second C. 10 mmol per litre / second D. 60 mmol per litre / secondarrow_forward1/v (sec/μmol) Enzymes A and B catalyze different reactions but use the same reactant molecule as a substrate. The graph below presents the double-reciprocal plots observed when enzyme A and enzyme B are mixed together in a single test tube containing molecule X. X 12° 1> 0.45 0.40 Y 0.35 0.30 Z 0.25 0.20 0.15 0.10 2.05 0.00 -1.20 -1.00 -0.80 -0.60 -0.40 -0.20 0.00 0.20 0.40 0.60 0.80 1.00 1.20 1/[X] (1/μM) A-B What are the Vmax and the Km values for each enzyme under these conditions? A Vmax = 5.9 μmol sec KM = 1.00 μΜ B Vmax = 10. μmol sec KM = 3.0 μΜarrow_forward1. Explain the biochemical role of the phosphate that is removed in reaction B. 2. What would be a typical functional group for a similar reaction in an organic lab? 3. Name the primary enzyme class for the reactions B, C, D1, and F. 4.Indicate the name of the primary enzyme and subclass for reaction E? 5. Explain the reversible reactivity of NADH and NAD+ based on the core structure and provide one chemical equivalent for each of them.arrow_forward
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