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

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

The substrate concentration that gives 50% of the maximum velocity

What does Vmax represent in the Michaelis Menten model?

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

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

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

The enzyme has high catalytic activity

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

At excessively high concentration of substrates

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

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

To find the Vmax

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

Affinity of the enzymes for the substrate

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

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

Kcat remains constant

How can Vmax be found using the MM graph?

By finding the x-intercept of the MM graph

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

They are equal in value

What does the specificity constant describe?

The ratio between Kcat and Km

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

Vmax is an unknown asymptote

What aspect of enzyme performance does a low Km indicate?

High affinity for substrate

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

Km is inversely proportional to Kcat

Explore the regulation and biological catalysts of enzymes in this lecture covering the Michaelis Menten Model and its implications on enzyme kinetics. Understand the relationship between enzyme and substrate concentrations and the concept of Vmax.

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