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Chemical Reaction Rates and Kinetics Study

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Questions and Answers

What happens at low substrate concentrations in allosteric enzymes?

The R form becomes more prevalent
There is little enzyme activity (correct)
Multiple substrates bind simultaneously to the enzyme
It is easier for substrate to bind to the T form

How does cooperativity affect enzyme activity in allosteric enzymes?

It decreases the velocity of the reaction significantly
It causes substrates to unproductively collide with the enzyme
Only one substrate can bind to the enzyme at a time
It leads to a sharp increase in reaction velocity in the middle of the curve (correct)

How do positive effectors modulate allosteric enzymes?

They make it more difficult for substrate to bind
They lower the threshold concentration level of substrate needed for activity (correct)
They shift the curve to the right if activators
They bind to the T form to stabilize it

What are heterotropic effects on allosteric enzymes?

Shift the curve to the left if inhibitors (D) Signup and view all the answers

How does the Sequential Model account for allosteric effects?

Each site of the enzyme changes as soon as one substrate binds (A) Signup and view all the answers

What is the effect of negative effectors on allosteric enzymes?

They raise the threshold concentration level of substrate needed for activity (D) Signup and view all the answers

What distinguishes allosteric enzymes from Michaelis-Menten enzymes with respect to sensitivity to substrate concentration?

Allosteric enzymes require less change in substrate concentration for a given change in velocity near KM (B) Signup and view all the answers

How do homotropic effects differ from heterotropic effects on allosteric enzymes?

Homotropic effects involve effects of regulatory molecules on allosteric enzymes (C) Signup and view all the answers

What characterizes enzyme behavior according to the text?

Most enzymes exhibit a combination of sequential and concerted models (C) Signup and view all the answers

What is a characteristic of an R form in allosteric enzymes?

It stabilizes active sites in a way that makes substrate binding easier (A) Signup and view all the answers

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