Ch. 7 - Enzyme Inhibition and Regulation WorksheetSee 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
Enzyme Inhibition
Irreversible Inhibition
Reversible Inhibition
Inhibition Constant
Degree of Inhibition
Apparent Km and Vmax
Inhibition Effects on Reaction Rate
Competitive Inhibition
Uncompetitive Inhibition
Mixed Inhibition
Noncompetitive Inhibition
Recap of Reversible Inhibition
Allosteric Regulation
Allosteric Kinetics
Allosteric Enzyme Conformations
Allosteric Effectors
Concerted (MWC) Model
Sequential (KNF) Model
Negative Feedback
Positive Feedback
Post Translational Modification

Concept #1: Allosteric Enzyme Conformations

Concept #2: T State & R State

Concept #3: Allosteric Constant (L0)

Practice: Which of the following is true about allosteric enzyme conformational states?

Concept #4: T/R Conformations Allow for Cooperative Kinetics

Concept #5: L0 Dictates Curve in Kinetics Plots

Practice: An allosteric enzyme that follows the concerted model mechanism has a L 0 = 10,000 in the absence of substrate. A mutation in this enzyme caused the L0 to now be 1/10,000 (reciprocal to its original value). What affect does this mutation have on the reaction rate of the enzymatic reaction?