1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false

1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
1. Activatotrs are types of A. inhibitor B. cofactor C. enzyme D. substrate 2. Which of the following does NOT affect enzyme selectivity ? A. Electrostatic interactions B. Molecular shape C. hydrophillic Interactions D. None of these answers are correct
A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme B
Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
1. How much faster is a reaction with the faster enzyme than without a catalyst? * A. Approximately 10 times faster. B. About 100 times faster. C. Approximately 1,000 times faster. D. About 10,000 times faster. E. About 10X^20 times faster. 2. For competitive inhibition * A. KM value decreases B. the value of Vmax decreases C. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate D. None of the above
A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.
Which one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.
1. There are two major categories of enzyme, inhibition, name, and describe them. 1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.
Item 35 Organic cofactors are referred to as _________. Fill in the blank Item36 Item Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e. substrate, and its effectiveness depends on product concentration. Item37 Item 37 A substance that binds to the active site of an enzyme and turns it off is called a _________ inhibitor. Fill in the blank Item 38 Lactase is an enzyme that digests lactose. True or False Item 39 Exergonic reactions do not require activation energy. True or False
Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.