Chapter 3: Enzymes Flashcards

(52 cards)

1
Q

How to measure the initial rate of reaction?

A
  1. Where does it look most linear?
  2. Find the (x,y)
  3. Slope = (change in y/change in x)
  4. Example: x=10, y=6
  5. (6-0/10-0)
  6. 6/10
  7. initial rate of reaction 0.6 mol
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2
Q

Explain the effect of enzyme concentration on enzyme activity.

A

As enzyme concentration increases, the initial rate of reaction increases.

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3
Q

Why does the initial rate of reaction increase as enzyme concentration increases?

A

More enzymes = more active sites

More active sites = more places for substrate molecules to bind to

More substrate molecules bound to active sites = more product produced quicker

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4
Q
A
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5
Q

Explain the effect of substrate concentration on enzyme activity.

A

As substrate concentration increases, reaction rate will increase but only to a point.

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6
Q

point of enzyme-saturation

A

all active sites are engaged

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7
Q

How to determine velocity

A

The rate at which the active site can convert SUBSTRATE —-> PRODUCT

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8
Q

Explain the effect of temperature on enzyme activity.

A

As temperature increases, reaction rate will increase but only to a point. Once the temperature exceeds the optimal temperature for enzyme activity, reaction rate will decrease.

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9
Q

What is the optimal temperature for most human enzymes?

A

35-40*C

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10
Q

What happens to enzymes and substrates when temperature increases ?

A

They move faster, making it more likely for them to collide with one another

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11
Q

What happens if the temperature gets too high?

A

The enzyme vibrates SO rapidly that they denature. This DESTROYS the active site

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12
Q

Denature

A

Loses their tertiary shape

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13
Q

What happens when all the enzymes have denatured?

A

The reaction stops

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14
Q

What happens to enzymes during cold temperatures?

A

They do not denature they just move slowly

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15
Q

Explain the effect of pH on Enzyme activity.

A

As pH decreases or increases from the optimum, reaction rate will decrease.

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16
Q

The optimal pH of most human enzymes

A

pH 6-8

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17
Q

When do enzymes denature from pH.

A

acidic or basic conditions denature most enzymes

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18
Q

Explain the effect of inhibitors on enzyme activity.

A

inhibitors are molecules that interfere with the normal functioning of enzymes and slow down or stop enzyme activity

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19
Q

What are the two main types of inhibitors.

A

competitive and noncompetitive

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20
Q

What are competitive inhibitors

A

They are similar to enzyme’s substrate and binds to the active site.

•similar to enzyme
•binds to active site

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21
Q

What are noncompetitive inhibitors

A

They are not similar to the enzyme’s substrate and do not bind to the active site
•not similar to substrate
•do not bind to active site

22
Q

Where do noncompetitive inhibitors bind to?

A

an alternative site

23
Q

What do noncompetitive inhibitors do to the enzyme when they bind to the alternative site

A

They alter the shape of the active site and the substrate can’t bind to it

24
Q

What happens when you increase the concentration of an inhibitor?

A

the rate of reaction reduces and the reaction can completely stop at very high concentrations of inhibitors

25
How is the effect of competitive inhibitors overcome?
increasing the substrate concentration ---> increases the chance of enzymes to collide with substrates rather than inhibitors
26
How is the effect of noncompetitive inhibitors overcome?
It cannot be overcome. Once the noncompetitive inhibitor binds to the alternative site the effect is permanent to the enzyme. It reduces the # of functional enzymes
27
What does Vmax mean
the maximum speed at which an enzyme works
28
What happens at Vmax?
All available enzymes have substrate bound to their active sites
29
how is Vmax measured
keeping the enzyme concentration constant and increasing the substrate concentration
30
When is Vmax reached after measuring it?
When adding additional substrate no longer increases the rate of product formation
31
What is Km
the affinity of an enzyme for its substrate
32
what is affinity
attraction
33
What happens when the affinity is greater
the more likely it is that product will be formed when a. substrate molecule enters an enzymes active site
34
What happens when the affinity is lower
the less likely it is that product will be formed when an a substrate molecule enters an enzymes active site
35
Can a substrate leave before making product
Yes, it may leave the active site before a reaction takes place
36
How to calculate Km?
Since Km is equal to the substrate concentration at which an enzyme works at half its rate then... 1/2 Vmax
37
(affinity)The lower the substrate concentration needed for an enzyme to reach 1/2Vmax the ....
the higher affinity it has for its substrate
38
as Km decreases, the affinity for an enzyme for its substrate....
increases
39
Does VMax change in competitive inhibition
vmax does not change.
40
Why does Vmax not change in competitive inhibition at high concentrations of substrate
The inhibitor is not noticed by the enzyme allowing the enzyme to bind to its substrate and work like "normal"
41
Does Km increase or decrease in competitive inhibition?
Km increases because competitive inhibitors reduce the likelihood of enzymes interactive with substrates so it takes more substrate to reach 1/2Vmax
42
Does Vmax stay the same during noncompetitive inhibition?
No, Vmax decreases because it depends on the enzyme concentration and in presence of a noncompetitive inhibitor, the number of active enzymes is reduced
43
Does Km change during noncompetitive inhibition?
no because the enzymes that are active still have the same affinity as they normally do
44
What are immobilized enzymes?
immobilized enzymes are enzymes that have been fixed to a surface or trapped inside agar beads
45
What happens when enzymes are trapped inside agar beads or fixed to a surface
They cannot move around, they are immobile
46
What are the advantages of using immobilized enzymes commercially?
• allows them to be reused many times • keeps the product enzyme-free • more tolerant of temperature and pH changes
47
Why is it important for immobilized enzymes to be more tolerant of temperature and pH changes?
processes can be run at higher temperatures allowing product to be made at a faster rate
48
How do immobilized enzymes work?
1. Immobilizing the enzyme (lactase) 2. Using the immobilized lactase to product lactose-free milk 3. Advantages
49
How to immobilize lactase?
1. mix lactase into a solution of sodium alginate 2. little droplets of this mixture are added to a solution of calcium chloride 3. calcium chloride and sodium alginate react instantly to form a jelly like substance 4. thus, each droplet forms a little bead
50
How to immobilize lactase to product lactose-free milk
1. the alginate beads containing the immobilized enzyme are packed into a column 2. milk is added to the column 3. as milk runs through the column over the surface of the beads, the lactase in the beads catalyze the hydrolysis of lactose into glucose and galactose 4. lactose free milk emerges from the bottom of the column
51
Advantages of producing lactose free milk using immobilized lactase
• the lactose-free milk is not contaminated with the enzyme lactase • the same batch of immobilized lactase can be used over and over again to produce a large volume of lactose free milk
52