Practice: To determine the Km from a Lineweaver-Burk plot you would:
Subjects
Sections | |||
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Enzymes | 25 mins | 0 completed | Learn |
Enzyme-Substrate Complex | 21 mins | 0 completed | Learn |
Lock and Key Vs. Induced Fit Models | 24 mins | 0 completed | Learn |
Optimal Enzyme Conditions | 12 mins | 0 completed | Learn |
Activation Energy | 31 mins | 0 completed | Learn |
Types of Enzymes | 43 mins | 0 completed | Learn |
Cofactor | 16 mins | 0 completed | Learn |
Catalysis | 25 mins | 0 completed | Learn |
Electrostatic and Metal Ion Catalysis | 11 mins | 0 completed | Learn |
Covalent Catalysis | 23 mins | 0 completed | Learn |
Reaction Rate | 11 mins | 0 completed | Learn |
Enzyme Kinetics | 24 mins | 0 completed | Learn |
Rate Constants and Rate Law | 36 mins | 0 completed | Learn |
Reaction Orders | 52 mins | 0 completed | Learn |
Rate Constant Units | 12 mins | 0 completed | Learn |
Initial Velocity | 34 mins | 0 completed | Learn |
Vmax Enzyme | 27 mins | 0 completed | Learn |
Km Enzyme | 42 mins | 0 completed | Learn |
Steady-State Conditions | 29 mins | 0 completed | Learn |
Michaelis-Menten Assumptions | 18 mins | 0 completed | Learn |
Michaelis-Menten Equation | 52 mins | 0 completed | Learn |
Lineweaver-Burk Plot | 47 mins | 0 completed | Learn |
Michaelis-Menten vs. Lineweaver-Burk Plots | 20 mins | 0 completed | Learn |
Shifting Lineweaver-Burk Plots | 37 mins | 0 completed | Learn |
Calculating Vmax | 45 mins | 0 completed | Learn |
Calculating Km | 31 mins | 0 completed | Learn |
Kcat | 47 mins | 0 completed | Learn |
Specificity Constant | 62 mins | 0 completed | Learn |
Concept #1: Calculating Km with Algebra
Concept #2: Calculating Km with Reaction Rates
Example #1: The following rate constants were measured for a simple enzyme-catalyzed reaction. Determine the Km.
Practice: To determine the Km from a Lineweaver-Burk plot you would:
Practice: The Vmax for an enzyme is 9 mg/min. Calculate the Km if the [S] = 5 mM when the V0 = 3 mg/min.
Practice: Calculate the Km of an enzyme using Michaelis-Menten kinetics if the forward rate constant for ES formation is 4.3 x 106 M-1s-1, the reverse rate constant for ES dissociation into E + S is 2.4 x 102 s-1, and the forward rate constant for ES dissociation into E + P is 1.2 x 10 3 s-1.
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