Enzymes Flashcards

(51 cards)

1
Q

What is a catalysis?

A

Study of how fast chemical reactions proceed

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

What is a catalyst?

A

A substance that increases the rate of chemical reactions

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

How do catalysts act?

A

By reducing the activation energy of a chemical reaction

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

What are enzymes?

A

Proteins which are biochemical catalysts

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

Relative specificity

A

Acting on several structurally related substances

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

Absolute specificity

A

Acting on one and only one substance

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

Stereochemical specificity

A

Acting on a specific stereoisomer

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

What can be regulated?

A

The catalytic behavior of an enzyme

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

What are coenzymes?

A

Organic molecules that act as cofactors

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

What are cofactors

A

Small organic molecules and ions (Zn, Co, Fe)

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

When can enzymes be catalytically active?

A

Only if a specific group or cofactors is attached to them

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

What makes an active enzyme?

A

Apoenzyme and cofactor (coenzyme or ion)

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

What is an active site?

A

Location on an enzyme where a substrate is bound to initiate catalysis

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

When does a binding of a substrate to the active site occur?

A

By matching intermolecular forces

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

What happens when an enzyme binds to a substrate?

A

Is forms an enzyme-substrate complex which releases a product

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

What is the lock-and-key model?

A

When the rigid enzyme and substrate have matching shapes.
Active site + substrate= EXACT FIT

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is the induced-fit model?

A

When the flexible enzyme changes shape to match the substrate.
Active site ADJUSTS to fit substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is the enzyme activity?

A

The rate at which an enzyme catalyzes a reaction.
=speed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is the turnover number?

A

The number of molecules of substrate acted on by one molecule of enzyme per minute.
=the amount

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What factors affecting enzyme activity are due to kinetics ?

A

Enzyme and substrate concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What factors affecting enzyme activity are affecting the structure of an enzyme?

A

Temperature and pH

22
Q

Enzyme concentration

A

Increase the number of enzyme

23
Q

Substrate concentration

A

Increase substrate, reach max velocity

24
Q

What happens when you increase temperature?

25
What is an ezyme inhibitor?
A substance that decreases the rate of an enzyme-catalyzed reaction.
26
What is an irreversible inhibition?
Forms. Strong bond with a specific functional group of an enzyme rendering it inactive. (Kills enzymes)
27
Reversible inhibition
Competitive and in competitive inhibitor
28
Competitive inhibitor
Substrate + inhibitor takes the same spot in the enzyme.
29
How to restore the activity of the enzyme?
By adding more substrate
30
Noncompetitive inhibitor
- Binds to the enzyme at a location other than the active site - cannot be reversed by adding more substrate - often changes the active site of the enzyme
31
Activation of zymogens (proenzymes)
Inactive precursor of an enzyme
32
Why are enzymes released in an inactive form?
To become fully active only when needed
33
What happens when enzymes perform functions if they were released in an active form?
It could degrade cell components
34
Allosteric regulation
Uses allosteric enzyme and modulator
35
Allosteric enzyme
An enzyme whose activity is changed by the binding of modulators
36
What is a modulator
A substance that binds to an enzyme at a location other than the active site and alters it’s catalytic activity.
37
Example of Allosteric regulation
Final product becomes a noncompetitive inhibitor of an early enzyme in the pathway for biosynthesis of isoleucine.
38
Genetic control
The synthesis of proteins is under genetic control
39
Example of genetic control
Enzyme induction : synthesis of enzymes in response to a temporary need of the cell
40
When cells are damaged or die, what do enzymes do?
Reside inside the cells and are released
41
How to detect a condition in the concentration of enzymes in blood?
If level goes up. Usually, the level remains low
42
Isoenzymes
Slightly different form of the same enzyme produced by different tissues (ex: LDH)
43
What is used in the diagnosis of a wide range of diseases!
Serum levels of LDH due to the difference in tissue distribution of LDH isoenzymes.
44
Alkaline phosphate (ALP)
Liver or bone disease
45
Amylase
Pancreas disease
46
Creatinine phosphokinase
Heart attack
47
Aspartate transaminase (AST)
Liver and/or heart attack
48
Alanine transaminase (ALT)
Hepatitis
49
Lactate dehydrogenase (LDH) l
Liver and/or heart attack
50
Lipase
Acute pancreatitis
51
Lysozyme
Monocytic leukemia