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Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = Km/Vmax Intercept = -1/KM Intercept = 1/Vmax 1/[S] % (µmol/min); with no V (µmol/min); with Vo (µmol/min); with [S] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).

Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = Km/Vmax Intercept = -1/KM Intercept = 1/Vmax 1/[S] % (µmol/min); with no V (µmol/min); with Vo (µmol/min); with [S] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).

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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Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.

Substrate concentration, [S], has units of micromolar, μM.

Enzyme velocity, ?0, has units of micromole per minute, (μmol/min).
Using data from only the extremes of the [S] range is unreliable.

Select the type of inhibition displayed by inhibitor A.

  1. competitive
  2. noncompetitive
  3. uncompetitive

Select the type of inhibition displayed by inhibitor B.

  1. competitive
  2. noncompetitive
  3. uncompetitive
Vmax; no inhibitor = µmol/min KM: no inhibitor = µM umol/min KM: with inhibitor A uM max; with inhibitor A umol/min KM: with inhibitor B uM max; with inhibitor B Select the type of inhibition displayed by inhibitor A. Select the type of inhibition displayed by inhibitor B. O competitive competitive noncompetitive noncompetitive uncompetitive uncompetitive
Transcribed Image Text:Vmax; no inhibitor = µmol/min KM: no inhibitor = µM umol/min KM: with inhibitor A uM max; with inhibitor A umol/min KM: with inhibitor B uM max; with inhibitor B Select the type of inhibition displayed by inhibitor A. Select the type of inhibition displayed by inhibitor B. O competitive competitive noncompetitive noncompetitive uncompetitive uncompetitive
Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = KM/Vmax %3D Intercept = -1/KM Intercept = 1/Vmax 1/[S] Vo (umol/min); with no Vo (umol/min); with Vo (µmol/min); with IS] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 5 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min). Using data from only the extremes of the [S] range is unreliable.
Transcribed Image Text:Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = KM/Vmax %3D Intercept = -1/KM Intercept = 1/Vmax 1/[S] Vo (umol/min); with no Vo (umol/min); with Vo (µmol/min); with IS] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 5 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min). Using data from only the extremes of the [S] range is unreliable.
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