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Ch. 6 - Enzymes and Enzyme KineticsWorksheetSee all chapters
All Chapters
Ch. 1 - Introduction to Biochemistry
Ch. 2 - Water
Ch. 3 - Amino Acids
Ch. 4 - Protein Structure
Ch. 5 - Protein Techniques
Ch. 6 - Enzymes and Enzyme Kinetics
Ch. 7 - Enzyme Inhibition and Regulation
Ch. 8 - Protein Function
Ch. 9 - Carbohydrates
Ch. 10 - Lipids
Ch. 11 - Biological Membranes and Transport
Ch. 12 - Biosignaling
Clutch Review 1: Nucleic Acids, Lipids, & Membranes
Clutch Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway
Clutch Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism
Clutch Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation
Sections
Enzymes
Enzyme-Substrate Complex
Lock and Key Vs. Induced Fit Models
Optimal Enzyme Conditions
Activation Energy
Types of Enzymes
Cofactor
Catalysis
Electrostatic and Metal Ion Catalysis
Covalent Catalysis
Reaction Rate
Enzyme Kinetics
Rate Constants and Rate Law
Reaction Orders
Rate Constant Units
Initial Velocity
Vmax Enzyme
Km Enzyme
Steady-State Conditions
Michaelis-Menten Assumptions
Michaelis-Menten Equation
Lineweaver-Burk Plot
Michaelis-Menten vs. Lineweaver-Burk Plots
Shifting Lineweaver-Burk Plots
Calculating Vmax
Calculating Km
Kcat
Specificity Constant

Concept #1: Steady State Conditions

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Concept #2: Pre-Steady-State

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Concept #3: Steady-State Conditions

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Practice: True or false: A reaction system at steady-state must also be at equilibrium.

Concept #4: Km and Michaelis-Menten-Equation are Derived under Steady-State

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Practice: The steady state assumption, as applied to enzyme kinetics, implies:

Practice: Draw the curves that show the appropriate relationships between the variables in each of the plots below for a simple enzyme-catalyzed reaction that follows Michaelis-Menten kinetics.

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