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ENZYME Packet

Notes for AP Biology

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Lucinda Supernavage
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38 views

ENZYME Packet

Notes for AP Biology

Uploaded by

Lucinda Supernavage
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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Enzymes

ENZYME VIDEO LECTURE


3.1 Enzyme Structure
Objective: Describe the properties of enzymes.
3.2 Enzyme Catalysis
Objective: Explain how enzymes affect the rate of biological reactions.

Directions: watch the Bozeman video linked in the Cell Energy Module and
complete the video guide below:

1. What reaction does catalase catalyze? Write out the balanced chemical equation.

2. How fast does catalase work?

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

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


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

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

7. What is the interaction between the active site and the substrate?

8. What is the advantage to using an enzyme?

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

10. What are the two types of activators?


11. Define cofactor and give an example of one.

12. Define coenzyme and give an example.

13. Describe competitive inhibition.

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


competitive inhibition.

15. What is the allosteric site?

16. What are two possible ways that allosteric inhibitors affect the action of the
enzyme?
17. How does temperature affect enzyme activity?

ENZYME CATALYSIS & DENATURATION


3.3 Environmental Impacts on Enzyme Function
Objective: Explain how changes to the structure of an enzyme may affect its
function.
Objective: Explain how the cellular environment affects enzyme activity.
Lactase
Milk is packed with proteins, fats, and carbohydrates that support the
growth, development, and survival of baby mammals. The main carbohydrate
in milk is a disaccharide-sugar called lactose. To digest milk, lactose must be
cleaved, or broken down, by lactase, an enzyme produced in the small
intestine. Lactase cleaves lactose into two smaller sugars, glucose and
galactose, which are easily absorbed through the walls of the small intestine.
Once these sugars are absorbed into the bloodstream, they can be delivered
to the cells of the body and used for energy.

As baby mammals grow up and stop drinking their mother’s milk, their bodies
usually stop producing the lactase enzyme (presumably because it is no
longer needed). Individuals that do not produce lactase as adults are called
lactase non-persistent. Most mammals are lactase non-persistent and do
not drink milk as adults. Humans are unusual in that some adults continue to
drink milk from other mammals, such as cows. When an individual who is
lactase non-persistent drinks milk, they cannot easily break down the lactose
in the milk. The lactose passes from their small intestine to their large
intestine, where it is fermented by bacteria. Fermentation produces various
gases in the large intestine, which can cause abdominal pain, bloating,
flatulence, and diarrhea — all symptoms of lactose intolerance, the inability
to digest lactose. Most adults are lactase non-persistent and thus typically
lactose intolerant (although some may not know it because their symptoms
are mild). However, about 35% of the global human population continues to
produce lactase into adulthood. These individuals are called lactase
persistent and are typically lactose tolerant, meaning that they can digest
lactose easily and drink milk without problems.

There are several ways to test whether someone is lactase persistent or


nonpersistent. One method is the blood glucose test. Table 1 shows the blood
glucose levels of 7 individuals over time. The glucose levels were measured
using glucose strips and a glucose reader. After baseline levels (i.e., the ones
at “0 minutes”) were measured, each person drank a liter of milk. Their blood
glucose levels were measured again at 15, 30, 45, and 60 minutes after
drinking the milk. Plot the data in Table 1 below using different colored lines.
Be sure to add them to the key.
1. Why might someone’s blood glucose levels after drinking milk indicate
their lactase activity?

2. Divide the individuals in Table 1 into two groups (A and B) based on


their blood glucose test results. Write the names of the individuals in
each group, including Spencer Wells, below.
Group A Group B

3. Do you think the individuals in Group A are lactase persistent or non-


persistent? Why?

4. Do you think the individuals in Group B are lactase persistent or non-


persistent? Why?
5. If the blood glucose test was performed on people from the Maasai
population in Kenya, would their results be more like those of the
individuals in Group A or Group B? Explain your prediction.

6. A person taking a blood glucose test is usually told to fast (i.e., to not
eat or drink anything but water) before the test. Why do you think that
might be necessary?

Another common way to test whether a person is lactase persistent or


nonpersistent is the hydrogen breath test. This test uses the amount of
hydrogen in a person’s breath to check for lactose fermentation. As
described in the “Background” section, undigested lactose is fermented by
bacteria in the large intestine. Fermentation produces several gases,
including hydrogen, that can exit the body through the anus. These gases can
also be absorbed into the blood, circulated to the lungs, and eliminated
through the breath.

Table 2 shows the levels of hydrogen in the breath of four adults tested for
lactase persistence. As in Table 1, the measurements at “0 minutes” represent
baseline levels before drinking milk. The other measurements were taken at
various times after drinking milk.

Create your own graph below and determine which individuals are lactase
persistent and which are non persistent. Explain your reasoning.
toothpickase
Part A: Control/Baseline

# of molecules
Time
hydrolyzed
(seconds)
CUMULATIVE
20
40
60
80
100

Part B: Partial Enzyme Denaturation


Same procedure as the baseline, except with a sock
on your hand. Prediction?

Time # of molecules
hydrolyzed
(seconds)
CUMULATIVE
20
40
60
80
100
Part C: Competitive Inhibition
Same procedure as the baseline, except including
plastic toothpicks in the mix. Prediction?

# of molecules
Time
hydrolyzed
(seconds)
CUMULATIVE
20
40
60
80
100

Part D: Increasing Enzyme Concentration


Same procedure as the baseline, but now use
both hands. Prediction?

# of molecules
Time
hydrolyzed
(seconds)
CUMULATIVE
20
40
60
80
100
Analysis: type, answer in FULL SENTENCES, and share with me.
1. Describe the changes you see in each of your graphs.
2. In these activities, what object represents the enzymes?
3. What represents the active site?
4. What object represents the substrate?
5. What object represents the inhibitor?
6. In what way(s) was this simulation different from the enzymatic activity in a
cell? HINT: How did you find the appropriate substrate? How could you
modify the exercise to more accurately reflect enzyme-substrate interaction
within the cytoplasm?
7. In Part B, what happened to the efficiency of the enzyme’s activity? Explain
this
8. in light of enzyme structure and function.
9. What if you were asked to bounce a tennis ball twice before interacting with
your substrate? What does this represent for enzyme activity?
10. What if you put your hand in ice water for 5 minutes? How would that affect
enzyme activity?
11. What would happen to the reaction rate if the toothpicks were really spread
out? Why?

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