Chemical Kinetics and Enzyme Kinetics Study

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10 Questions

Which form of the allosteric enzyme do substrates bind more readily to?

R form

At low substrate concentrations, why is it difficult for substrate to bind to the T form of allosteric enzymes?

T form is less prevalent than R form

What effect does a positive effector have on the threshold concentration level of substrate needed for activity in allosteric enzymes?

Lowers the threshold concentration level

In allosteric enzymes, what effect do negative effectors have on the binding of substrates?

Decreases the binding of substrates

How do heterotropic effects influence the allosteric enzyme's reaction rate?

Increase the reaction rate

What does the sequential model propose about the structure changes in subunits of allosteric enzymes?

Only one subunit changes at a time as substrates bind sequentially

What effect does negative cooperativity have on the binding of additional substrate molecules in allosteric enzymes?

Inhibits binding of additional substrates

How do positive effectors affect the equilibrium between T and R forms of allosteric enzymes?

Shift towards R form

How does cooperativity affect enzyme activity in allosteric enzymes?

Increases enzyme activity due to substrate competition

What is the main difference between homotropic effects and heterotropic effects in allosteric enzymes?

Homotropic effects are solely due to substrate binding while heterotropic effects involve regulatory molecule binding.

Explore the concepts of chemical kinetics and enzyme kinetics, which involve studying the rates of chemical reactions and enzyme-catalyzed reactions. Learn about reaction velocity, rate constants, and first-order reactions.

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