BIOL 1020 - The Structure of ATP - Sundermann

What type of reaction breaks the bonds that join the phosphate groups in an ATP molecule?


Which part of the adenosine triphosphate molecule is released when it is hydrolyzed to provide energy for biological reactions?

?-phosphate (the terminal phosphate)

In general, enzymes are what kinds of molecules?


Enzymes work by _____.

reducing EA

An enzyme _____.

is an organic catalyst

What name is given to the reactants in an enzymatically catalyzed reaction?


As a result of its involvement in a reaction, an enzyme _____.

is unchanged

Which of the following is the strongest evidence that protein structure and function are correlated?

Denatured (unfolded) proteins do not function normally.

The process of cellular respiration, which converts simple sugars such as glucose into CO2 and water, is an example of _____.

a catabolic pathway

Which of the following terms most precisely describes the cellular process of breaking down large molecules into smaller ones?

catabolism (catabolic pathways)

Which of the following statements about anabolic pathways is true?

They consume energy to build up polymers from monomers

Which of the following statements is true for all exergonic reactions?

The reaction proceeds with a net release of free energy.

A chemical reaction that has a positive ?G is best described as _____.


Which of the following statements about ATP (adenosine triphosphate) is correct?

The cycling between ATP and ADP + Pi provides an energy coupling between catabolic and anabolic pathways.

Which of the following statements describes a central role that ATP plays in cellular metabolism?

ATP provides energy coupling between exergonic and endergonic reactions.

Which of the following molecules is most similar in structure to ATP?

an RNA nucleotide

Which of the following statements describes a common characteristic of catabolic pathways?

They are exergonic and provide energy that can be used to produce ATP from ADP and i

When chemical, transport, or mechanical work is done by an organism, what happens to the heat generated?

It is lost to the environment.

Enzymes are described as catalysts, which means that they _____.

increase the rate of a reaction without being consumed by the reaction

The binding of a compound to an enzyme is observed to slow down or stop the rate of the reaction catalyzed by the enzyme. Increasing the substrate concentration reduces the inhibitory effects of this compound. Which of the following could account for this

The compound is a competitive inhibitor.

Which of the following is true when comparing an uncatalyzed reaction to the same reaction with a catalyst?

The catalyzed reaction will have the same ?_G_.

Which of the following aspects of enzyme structure is best described by a clasping handshake analogy?

the specific manner in which an enzyme binds substrate

During a laboratory experiment, you discover that an enzyme-catalyzed reaction has a ?G of -20 kcal/mol. If you double the amount of enzyme in the reaction, what will be the ?G for the new reaction?

20 kcal/mol

How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?

by binding to an allosteric site, thus changing the shape of the active site of the enzyme

You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the reaction has stopped completely.
What can you do to regain the activity of the enzyme?

The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.

You have an enzymatic reaction proceeding at the optimum pH and optimum temperature. You add a competitive inhibitor to the reaction and notice that the reaction slows down.
What can you do to speed the reaction up again?

Add more substrate; it will outcompete the inhibitor and increase the reaction rate.