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

Allosteric Kinetics

Biochemistry

7. Enzyme Inhibition and Regulation

Allosteric Kinetics

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Multiple Choice

Because of the _____________ substrate-binding-site(s) & conformation(s) on an allosteric enzyme, the range of [S] to reach the V_max is _______________ for allosteric enzymes than it is for Michaelis-Menten enzymes.

Single, smaller.

Single, greater.

Multiple, narrower.

Multiple, wider.

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Verified step by step guidance

Understand that allosteric enzymes have multiple substrate-binding sites and can exist in multiple conformations, which affects their kinetic behavior.

Recognize that the Vmax (maximum velocity) of an enzyme is the rate at which the enzyme catalyzes a reaction when the substrate concentration is very high.

For allosteric enzymes, the presence of multiple binding sites and conformations means that the enzyme can be regulated by effectors, which can either activate or inhibit the enzyme's activity.

This regulation leads to a sigmoidal (S-shaped) curve when plotting reaction velocity against substrate concentration, as opposed to the hyperbolic curve seen in Michaelis-Menten kinetics.

As a result, the range of substrate concentrations ([S]) required to reach Vmax is wider for allosteric enzymes compared to Michaelis-Menten enzymes, due to the cooperative binding and regulation by effectors.