Chemistry A. Corti 10/01/2024 Lecture 7: Enzymes Pt2

Play an AI-generated podcast conversation about this lesson

What is the Michaelis Menten constant (Km) defined as?

The substrate concentration that gives 50% of the maximum velocity (correct)

The time required for the enzyme to catalyze a reaction

The concentration of the enzyme in a saturated solution

The maximum velocity of the enzyme-substrate reaction

What does Vmax represent in the Michaelis Menten model?

The amount of substrate required for the enzyme to catalyze a reaction

The maximum velocity that can be obtained when the enzyme is saturated by the substrate (correct)

The maximum enzyme concentration in a reaction

The time taken for the enzyme to reach its maximum activity

How is the Michaelis Menten Model different from the time course of an enzymatic reaction graph?

The MM graph includes time and product on the x and y axes, whereas the time course graph includes substrate concentration and reaction velocity (correct)

The MM graph represents the rate of an enzymatic reaction, whereas the time course graph represents enzyme concentration

The MM graph is used to calculate Km, whereas the time course graph is used to calculate Vmax

The MM graph shows the initial velocity, whereas the time course graph shows the final velocity

What can be inferred from a high Vmax in an enzyme-catalyzed reaction?

The enzyme has high catalytic activity Signup and view all the answers

In which scenario can Vmax be achieved in an enzyme-catalyzed reaction?

At excessively high concentration of substrates Signup and view all the answers

How is the Michaelis Menten graph used to understand enzyme kinetics?

It illustrates how the rate of an enzymatic reaction depends on the concentration of the enzyme and substrate Signup and view all the answers

What is the purpose of plotting the reciprocal of the MM graph?

To find the Vmax Signup and view all the answers

What information does the Michaelis Menten constant (Km) provide about the enzyme kinetics?

Affinity of the enzymes for the substrate Signup and view all the answers

What is the definition of turnover number/catalytic constant (Kcat)?

The number of substrate molecules converted into product in a unit time by one enzyme molecule Signup and view all the answers

What happens when the enzyme is totally saturated by the substrate, in relation to Kcat?

Kcat remains constant Signup and view all the answers

How can Vmax be found using the MM graph?

By finding the x-intercept of the MM graph Signup and view all the answers

What is the relationship between K2 and Kcat in the equilibrium equation?

They are equal in value Signup and view all the answers

What does the specificity constant describe?

The ratio between Kcat and Km Signup and view all the answers

Why is it difficult to evaluate the Michaelis Menten constant (Km) using the MM graph?

Vmax is an unknown asymptote Signup and view all the answers

What aspect of enzyme performance does a low Km indicate?

High affinity for substrate Signup and view all the answers

'Highly efficient enzymes have a high Kcat and a low Km' - What does this statement imply?

Km is inversely proportional to Kcat Signup and view all the answers

Chemistry A. Corti 10/01/2024 Lecture 7: Enzymes Pt2

Choose a study mode

Podcast

Questions and Answers