AP Bio 3.3

Question 1

What is the 3D shape of an enzyme called?

Answer 1

Tertiary structure, (or the conformational shape)

Question 1

What is denaturation?

Answer 1

Changes in the conformational shape of an enzyme

Question 2

What can lead to denaturation?

Answer 2

Changes in pH, and temperature.

Question 3

Is enzyme denaturation reversible?

Answer 3

Typically, no.

It’s ability is usually lost or severly decreased

Question 4

In some cases, is enzyme denaturation reversible?

Answer 4

Yas

Question 5

What is meant by the optimum temperature?

Answer 5

The ideal temperature for enzyme activity (fastest catalyzation)

Question 6

What happens when optimum ranges aren’t maintained

Answer 6

Reaction rates change

Question 7

What happens when temperatures exceed the optimum temperature for an enzyme?

Answer 7

An initial increase rate of reaction, molecular movement, and enzyme substrate collisions. Temperatures that are too high lead to denaturation.

Question 8

What happens when temperatures are less than the optimum temperature for an enzyme?

Answer 8

There is a decrease in the rate of reactions, but it does not lead to the denaturation of the enzyme or change in the enzymes structure

Question 9

What does pH measure?

Answer 9

It measures the concentration of hydrogen ions in a solution

Question 10

How is pH measured (mathematical wise)?

Answer 10

It is measured on a logartithmic scale

Small changes in pH equate to large changes in hydrogen concentration

pH 6 has 10x more hydrogen ions that pH 7

Question 11

What is meant by optimum pH?

Answer 11

it’s the ideal pH range for an enzyme to facilitate reactions (fastest reactions).

Question 12

What does a change in optimum pH level cause in an enzyme?

Answer 12

It causes either the slowing down or stopping of enzyme activity, as well as denaturation. Both high pH and low pH can lead to denaturation (if it’s outside of the optimum range)

Question 13

How can pH effect the structure of an enzyme?

Answer 13

The hydrogen ion concentration can effect the hydrogen bond interactions in the enzyme

Question 14

What does an increase in substrate do (when considering enzyme reactions)?

Answer 14

It generally means more reactions and more opportunity to collide with the enzyme

Question 15

What is something that will happen at some point in the reactions?

Answer 15

Substrate saturation

Question 16

What will happen to the saturation levels if the reaction rate is maintained?

Answer 16

The saturation levels are maintained

Question 17

What does an increased amount of products result in?

Answer 17

A decreased chance of new reactions occuring/the collision of substrates to the enzyme, slowing the reaction rate

Question 18

What is something that slows down the reaction rate of an enzyme?

Answer 18

The increased level of products in its surrounding environment

Question 19

Can changes in enzyme concentration change the reaction rate?

Answer 19

Yup

Question 20

What happens if there are more enzymes?

Answer 20

Faster reaction rate

More opportunities for the substrate to collide with the active site

Question 21

What happens if there are fewer enzymes?

Answer 21

Slower reaction rate

Fewer opportunities for the substrate to collide with the active site

Question 22

What are competitive inhibitors?

Answer 22

They are molecules that can bind reversibly or irreversibly to the active site of the enzyme, competing with the normal substrate for the enzymes active site

Question 23

What happens if competitive inhibitor concentrations are higher than the subsrate concentrations?

Answer 23

The reactions are slowed down

Question 24

What happens if competitive inhibitor concentrations are considerably lower than the subsrate concentrations?

Answer 24

The reactions can proceed normally

Question 25

What happens if an inhibitor binds irreversibly to the active site of an enzyme?

Answer 25

It’s activity will come to an end

Question 26

What happens when an inhibtor binds reversibly to the active site of an enzyme?

Answer 26

The enzyme can regain it’s ability to facilitate reactions once the inhibitor detaches

Question 27

What are the sites that can be found on an enzyme?

Answer 27

The active site, into which the subtrate binds in order for a reaction to be facilitated, along with the competitive inhibitors (to inhibit the binding of the substrate), and the allosteric site, onto which noncompetitive inhibitors may bind

Question 28

What’s an allosteric site?

Answer 28

It’s a site onto which noncompetitive molecules can bind in order to change the shape of the active site, preventing the attachment of substrates

Question 29

What happens if the concentration of the substrate increases in the presence of enzymes that have noncompetitive inhibitors attached to them?

Answer 29

Nothing will change, the enzymes will continue to be prevented from facilitating reactions because of the lack of attachment of substrates