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Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell? In Michaelis menton kinetics which variable is held constant? multiselect a. substrate concentration b. enzyme concentration c. reaction time Which of the following binds to the active site multiselect a. competitive inhibitor b. non-competitive inhibitor c. mixed inhibitor An enzyme with a high/strong affinity for substrate has multiselect a. low Km b. high Vmax c. x intercept close to the origin d. y intercept close to the origin The addition of an enzyme will make a non-spontaneous reaction spontaneous multiselect-just kidding True or False The addition of an enzyme can make a non-spontaneous reaction go True of False where would a second molecule be added during nucleic acid elongation (ie., syn- thesis) Nucleotide structure NH2 Phosphate Base O=P-0-CH20. HH OH H Sugar In the reversible reaction A – B; Keq (equilibrium constant) is а. [ВУ[A] b. [A]/[B] c. equal to 1 d. the difference between A and B

Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell? In Michaelis menton kinetics which variable is held constant? multiselect a. substrate concentration b. enzyme concentration c. reaction time Which of the following binds to the active site multiselect a. competitive inhibitor b. non-competitive inhibitor c. mixed inhibitor An enzyme with a high/strong affinity for substrate has multiselect a. low Km b. high Vmax c. x intercept close to the origin d. y intercept close to the origin The addition of an enzyme will make a non-spontaneous reaction spontaneous multiselect-just kidding True or False The addition of an enzyme can make a non-spontaneous reaction go True of False where would a second molecule be added during nucleic acid elongation (ie., syn- thesis) Nucleotide structure NH2 Phosphate Base O=P-0-CH20. HH OH H Sugar In the reversible reaction A – B; Keq (equilibrium constant) is а. [ВУ[A] b. [A]/[B] c. equal to 1 d. the difference between A and B

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell?
Transcribed Image Text:Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal enzyme Inhibitor A Convert these to lineweaver burke in graphs below. -5+ -4 Inhibitor B -3+ -2 Effect of Inhibitor A. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is A? How can you tell? Effect of Inhibitor B. Draw uninhibited first and then draw the result- ing inhibition for comparison. What kind of an inhibitor is B? How can you tell?
In Michaelis menton kinetics which variable is held constant? multiselect a. substrate concentration b. enzyme concentration c. reaction time Which of the following binds to the active site multiselect a. competitive inhibitor b. non-competitive inhibitor c. mixed inhibitor An enzyme with a high/strong affinity for substrate has multiselect a. low Km b. high Vmax c. x intercept close to the origin d. y intercept close to the origin The addition of an enzyme will make a non-spontaneous reaction spontaneous multiselect-just kidding True or False The addition of an enzyme can make a non-spontaneous reaction go True of False where would a second molecule be added during nucleic acid elongation (ie., syn- thesis) Nucleotide structure NH2 Phosphate Base O=P-0-CH20. HH OH H Sugar In the reversible reaction A – B; Keq (equilibrium constant) is а. [ВУ[A] b. [A]/[B] c. equal to 1 d. the difference between A and B
Transcribed Image Text:In Michaelis menton kinetics which variable is held constant? multiselect a. substrate concentration b. enzyme concentration c. reaction time Which of the following binds to the active site multiselect a. competitive inhibitor b. non-competitive inhibitor c. mixed inhibitor An enzyme with a high/strong affinity for substrate has multiselect a. low Km b. high Vmax c. x intercept close to the origin d. y intercept close to the origin The addition of an enzyme will make a non-spontaneous reaction spontaneous multiselect-just kidding True or False The addition of an enzyme can make a non-spontaneous reaction go True of False where would a second molecule be added during nucleic acid elongation (ie., syn- thesis) Nucleotide structure NH2 Phosphate Base O=P-0-CH20. HH OH H Sugar In the reversible reaction A – B; Keq (equilibrium constant) is а. [ВУ[A] b. [A]/[B] c. equal to 1 d. the difference between A and B
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