Clutch Prep is now a part of Pearson
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: Calculating Vmax

Expert Q&A

Ask unlimited questions and get expert help right away.

Concept #2: Recall: Initial Velocity and Vmax

Expert Q&A

Ask unlimited questions and get expert help right away.

Example #1: Calculate the maximum reaction velocity (Vmax) of an enzyme if the Km = 7 mM and the initial reaction velocity(V0) = 86.71 μM/sec when the [S] = 25 mM.

Expert Q&A

Ask unlimited questions and get expert help right away.

Practice: Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 104 s-1, what is the theoretical maximum reaction velocity for the enzyme?

Practice: For a Michaelis-Menten enzyme, what is the value of Vmax if at 1/10 Km, the V0 = 1 μmol/min.

Practice: Carbonic anhydrase catalyzes the hydration of CO2. The Km of carbonic anhydrase for CO2 is 12 mM. The initial velocity (V0) of the enzyme-catalyzed reaction was 4.5 μmole*mL-1*sec-1 when [CO2] = 36 mM. Calculate the Vmax of carbonic anhydrase.

Practice: Triose phosphate isomerase catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P) during glycolysis; however, this is a reversible reaction. The Km of the enzyme for G3P is 1.8 x 10 -5 M. When [G3P] = 30 μM, the initial rate of the reaction (V0) = 82.5 μmole*mL-1*sec-1. Calculate the Vmax.

Expert Q&A

Ask unlimited questions and get expert help right away.