AP Biology 048 – Enzymes

Video Review Sheet

www.bozemanscience.com/048-enyzmes

1. What are enzymes?

- Chemicals that are not consumed in a reaction but can speed up a reaction.

2. What reaction does catalase catalyze? Write out the balanced chemical equation.
- It breaks down hydrogen peroxide.
2H2O → 2H2O + O2

3. How fast does catalase work?

- 40 million H2O2 molecules broken down every second

4. What is the active site and what is its function?

- An area on the enzyme where the reaction occurs. It perfectly fits the substrate.

5. What kinds of regulation exist for enzymes? (2x)

- Activation (turn on enzyme)
- Inhibition (turn off enzymes)

6. What are the two types of inhibition? (2x)

- Two types of Inhibition are Competitive and Allosteric.

7. How do you measure the rate of an enzymatic reaction? (2x)

- Measure either the reactants or the product.

8. What is the interaction between the active site and the substrate? (They are like
a….)
- Substrate fits into the active site perfectly like a lock and key.

9. What is the advantage to using an enzyme?

- An enzyme lowers the activation energy.

10. How do we turn enzymes on? (2x)

 - Only produce the enzymes as needed and add something to an existing
enzyme to make it work

11. What are the two types of activators?

- To types of activators are Cofactors and Coenzyme

12. Define cofactor and give an example of one.

- Cofactor are small chemicals
Example: Heme

13. Define coenzyme and give an example.

- Coenzyme are small, organic chemicals
Ex. Thiamine

14. Describe competitive inhibition.

- An inhibitor that is a chemical. Blocks or binds the active site so the substrate
cannot fit in.

15. What is another name for non-competitive inhibition? Describe non-competitive

inhibition.
- Also called Allosteric, binds to the allosteric site to either change the shape of
the enzyme or active site.

Review Sheet for AP Biology 048 – Enzymes

Contributed by Winnie Litten — YouTube -­­
/mslittenbiology Twitter-­­@mslittenbiology

16. What is the allosteric site?

- Another site on the enzyme where an inhibitor can bind.
17. What are two possible ways that allosteric inhibitors affect the action of the
enzyme?
- Inhibitor binds to the allosteric site, blocks the active site and changes the
shape of the enzyme
- Inhibitor binds to the allosteric site and changes the shape of the active site.

18. What are the two ways that we can measure reaction rate.
- Measure the amount of product created
 - Measure the amount of reactant consumed.

19. What is the correlation between temperature and enzyme activity.

- The reaction speed increases util it
denatures