Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

7. Enzyme Inhibition and Regulation

Recap of Reversible Inhibition

Biochemistry

7. Enzyme Inhibition and Regulation

Recap of Reversible Inhibition

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Which of the following statements are true about enzyme inhibitors?

Competitive inhibitors change the slope of the Lineweaver-Burk line but not the y-intercept.

Noncompetitive inhibitors are a type of mixed inhibitor.

Uncompetitive inhibitors change Km & Vmax in a way to create a parallel Lineweaver-Burk line.

Noncompetitive inhibitors result in lines with increasing [I] to share the same x-intercept.

All the above are true.

Previous problemNext problem

Verified step by step guidance

Understand the role of enzyme inhibitors: Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. They can be classified into different types based on their mechanism of action.

Examine competitive inhibitors: Competitive inhibitors bind to the active site of the enzyme, competing with the substrate. In a Lineweaver-Burk plot, they increase the slope but do not affect the y-intercept, as they do not change Vmax but increase Km.

Explore noncompetitive inhibitors: Noncompetitive inhibitors bind to an allosteric site, not the active site, and can affect both Km and Vmax. They are a type of mixed inhibitor, as they can bind to the enzyme whether or not the substrate is present.

Analyze uncompetitive inhibitors: Uncompetitive inhibitors bind only to the enzyme-substrate complex, decreasing both Km and Vmax proportionally, resulting in a parallel shift of the Lineweaver-Burk plot.

Consider the effect of noncompetitive inhibitors on the Lineweaver-Burk plot: Noncompetitive inhibitors result in lines with increasing inhibitor concentration ([I]) that share the same x-intercept, as they do not affect Km.