C1.1: Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What type of proteins are enzymes?

A

Globular

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What do enzymes do?

A

Act as catalyst — speeds up the process but doesn’t alter the process

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Most proteins are..

A

enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What’s the suffix of enzyme name? Generally.

A

-Ase

e.g.:
Enzyme of sucrose is sucrase (sucrose -> fructose and glucose — breaks down because it’s a polysaccharide)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

How do enzymes work?

A

They weaken bonds which lowers activation energy
- E.g.: in catabolic reactions, if the bonds present are weakened, it would require less activation energy to start the reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Define activation energy

A

The energy to start a chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is an active site?

A

Where the substrate binds to enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What does the Induced Fit Model say?

A

The enzyme will adjust the shape of the active site to fit with the enzyme
But, *the enzyme will return to orig shape
like a desperate boyfie jk

-induced by the substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the area that’s not the active site?

A

Allosteric site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

How can the temperature affect enzymes? [4]

A

Generally: Thermal energy -> mvmt (KE) -> more collisions between substrate and enzyme;
- High temp: v enzyme stability = v hydrogen bonds of enzyme = enzyme loses shape;
- Low temp = v thermal energy = v enzymatic activity
- Optimal temp: *rate of enzyme @ peak
;

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Describe the two types of enzyme inhibitors

A

a.) Competitive inhibitors - chemicals resembling enzyme’s normal substrate and competes w/ actual for active site
- the substrate will just be misplaced but will be at active site after comp inhib
- just slow down the process but the process will still happen

b.) Non-competitive inhibitors - does not denature the enzyme but changes the shape of active site to avoid substrate to enzyme.
- makes the enzyme non-functional — denaturation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Differentiate the induced fit model vs the key and hole model

A

Induced fit model can hold more substrate because enzyme changes shape.

Key hole model says that the substrate and the enzyme have complimentary shapes in the beginning -> more rigid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are the two main types of metabolism?

A

1.) Anabolism
- simple -> complex (e.g. polymerization — condensation)

2.) Catabolism
- complex -> simple (ie. breaking down — hydrolysis)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Can enzymes only do catabolic reactions?

A

NO! They can do anabolic ones too!

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What do we call it when a substrate is bound to the enzyme?

A

Enzyme-substrate complex

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Give an example of the competitive inhibitors

A

Overactive people take medicine and the molecules (?) in the medicine blocks in the receptors of the brain cells

17
Q

Describe non-competitive inhibitors (Add Photo)

A

Enzyme inhibitors that bind to allosteric side
- Why? To change enzyme’s shape
- to alter the active site

18
Q

Describe the process of collision of substrate and enzyme?

A

Both move randomly but
The substrate is attracted to enzyme (polar-polar attraction),

Then the substrate is attached to enzyme via the active site

The enzyme catalyzes the reaction

19
Q

Define collision

A

The coming together of a substrate and enzyme

20
Q

Why is the cytoplasm the site of chemical reactions?

A

Because it is made out of fluids and thus contains water (water as solute property)

21
Q

What happens when substrate concentration > enzyme’s capacity?

A

There’s a plateau (constant enzyme activity) because the enzymes are occupied.
- The substrates can be accompanied, it’s just there’s a waiting line

22
Q

Why when there’s too high heat or to low heat, the chemical reaction/enzyme activity slows down? (ADD PHOTO)

A

Because it’s past/below the optimum temp
-> leads to denaturation (high heat = high energy = high mvmt -> the amino atoms of the enzymes will get excited and move and change the enzyme’s shape)
-> like “breaking”

23
Q

How does the pH range go?

A

1: most acidic
7: Neutral
8+: alkaline

24
Q

How to draw the optimum area in curved graphs?

A

The optimum area is the highest point and should be aligned with number.
-> for enzyme activity = start of curve

25
Q

Describe the relationship between energy and collision

A

^ thermal energy = ^ kinetic energy = ^ movement = ^ collision
- but if too hot, the enzyme will denature due to its sensitivity as a globular protein

26
Q

Evaluate this graph

A

0% Inhibitors - normal
25% Inhibitors - slower, but the enzymes are still working
50% Inhibitors - substrates have competition so lower enzyme activity compared to the others, the enzymes not occupied
- no plateau due to 50% chance of actual substrates binding

27
Q

Describe this graph of non-competitive inhibition

A

^ Increase in substrate concentration = v no. of enzymes able to accommodate them
- e.g. 25% inhibitor = 25% of enzymes not working — so still plateau, but later plateau than 50%

28
Q

How can heat cause denaturation

A

Its vibrations b=can break the intramoléculaire bonds

29
Q

Give practical examples of enzymes

A

1.) The enzymes in detergent breaking down the stains

2.) Paper production

3.) Food industry

4.) Brewing industry (e.g. enzymes used for beer)

5.) Medecine industry, etc

30
Q

Define carbohydrase

A

Enzymes of carbs

31
Q

Define lipase

A

enzymes of lipids

32
Q

Define proteases

A

Enzyme of protein

33
Q

Define amylase

A

a carbohydrase to break down starch

34
Q

Define immobilize

A

To make not move

35
Q

How can lactose-intolerant people drink milk and other dairy products?

A

They will use

36
Q

Define catalase

A

One of the most widespread enzymes that catalyzes the conversion of hydrogen peroxide

37
Q

How does pH affect enzymatic activity?

A

Change in pH = change in enzyme/denaturation = protein solubility + change in shape of molecule
- “^ change in shape = v binding w/ substrate”
- Different optimum pH for different enzymes (like temp)