Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biology > Module 2.1.4 Enzymes Sambrook > Flashcards

Module 2.1.4 Enzymes Sambrook Flashcards

1
Q

What is the turnover number ?

A

The number of reactions per enzyme per second

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

What are enzymes

A

-biological catalysts
- speed up metabolic reactions
- they remain unchanged

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

What are chemical catalysts?

A

-extreme in the following:
High Temp
High pressure
Ph

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

What are biological catalysts?

A

-low temp
-normal pressure
-neutral ph
-specific
-catalyse in both directions

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

What are enzymes made of?

A

-proteins (amino acids)

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

What does a gene mutation do to amino acid sequence of enzymes?

A

-no change as it’s degenerative
Or
-keep the protein the sme but change the structure
Or
-change the sequence enough so a totally different protein is made

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

What is the primary structure of enzymes?

A

The amino acid sequence

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

What is the secondary structure of enzymes?

A

Spiralling of the polypeptide

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

What is the tertiary structure of enzymes?

A

Folding of the polypeptide including the bonds between them giving the protein it’s specific shape-> including the active site

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

What is the quaternary structure of enzymes?

A

Multiple polypeptide chains jones together

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

Examples of metabolic disorders

A

-Tay sachs disease
-maple syrup urine disease
- phenylketonuria

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

Examples of structural disorders

A

-elhers danlos syndrome
-stone man syndrome

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

What are the 2 parts of the ACTIVE site?

A

-binding site
-catalytic site

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

What does the binding site do?

A

Bind and orient the substrate

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

What does the catalytic site do?

A

Puts pressure on the bonds-> reduces repulsion’s -> lowers the activation energy

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

How do enzymes lower the activation energy?

A

-put pressure on the bonds in the substrate when they bind to the active site
-this reduces the repulsion between the 2 substrate molecules holding them together allowing them to make a larger molecule

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

Explain the induced fit model

A
  • substrate binds to the active site
    -active site has a CONFORMATIONAL change
    -if another substrate were to enter the active site it would not bind in the correct places so would not cause this change
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What are intracellular enzymes?

A

Enzymes that act within the cell

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

Catabolic definition

A

Metabolic pathways that BREAKDOWN molecules

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

Anabolic definition

A

Metabolism pathways that SYNTHESISE larger molecules

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

What are intermediate substrates ?

A

Products of enzyme reactions that become substrates in another reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is catalase?

A

-an enzyme found in living organisms that is exposed to oxygen
-hydrogen is produced but must be broken down

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What are extra cellular enzymes?

A

Enzymes that act outside the cell

24
Q

Explain enzyme action

A

-Mucor release hydrolytic enzymes from their hyphae that digest carbs, lipids and proteins
- the products are then reabsorbed into the hyphae

25
What does catalase do?
Breaks down hydrogen peroxide to oxygen and water
26
What’s a prosthetic group ?
-A non protein group that is part of a protein
27
What is a cofactor?
A non- protein molecule that has to be present for an enzyme catalysed reaction to happen
28
Why are all prosthetic groups cofactors but not all cofactors are prosthetic groups ?
All prosthetic groups are permanently bound to the enzyme
29
Name for a red blood cell ?
Erythrocyte
30
What is carbonic anhydrase ?
Used in erythrocytes to catalyse the conversion of carbon dioxide and water to carbonic acid
31
What do temporary cofactors do?
-Some bind to the substrate to give it a complementary shape to the active site -some change the charges on the molecules which make it easier for bonds to form
32
What is a coenzyme?
Helps an enzyme carry out its function but is not used in the reaction itself
33
What happens to an enzyme above optimum temperature?
1)increased vibration breaks weak bonds 2)tertiary structure of the enzymes is changed 3)active site becomes denatured 4) substrate will no longer be able to bind to enzyme
34
How are optimum temperature and bonding related?
-the stronger the hydrogen and ion or bonds in the protein the higher the optimum temperature
35
What is psychrophilic bacteria
-cold loving bacteria
36
What is hyperthermophilic bacteria
Heat loving bacteria
37
Substrate rate of reaction calculation
1 ——————————————- Time taken to reach end point
38
Temperature coefficient calculation Q10
R2 rate of reaction at (T+10C) ——————————————— R1 Rate of reaction at TC
39
What are inactive precursors?
-enzymes that are only activated when they’re needed
40
What do inactive precursors do?
Stops reactions from happening when they are not needed or would be harmful.
41
What do inhibitors do ?
Reduce the activity of enzymes
42
How do inhibitors work?
-bind to the enzyme and effect the way the substrate can bind to the active site -by blocking the active site or causing a conformational change
43
Effect of ph on enzymes
-hydrogen and ionic bonds hold the tertiary structure of the protein -an excess of H+ or OH- ions can cause these bonds to break -this alters the active site and denatures the enzyme
44
Affect of substrate concentration on enzyme activity
-the greater the substrate concentration the higher the rate of reaction -as the substrate molecules increases the likelihood of enzyme substrate complex formation increases. -if enzyme concentration remains fixed but the amount of substrates increases all available active sites will become saturated -any further increase in substrate concentration will not increase reaction rate
45
Effect of enzyme concentration on enzyme activity
-the higher the enzyme concentration, the greater the number of active sits available -greater the likelihood of enzyme substrate complex formation. -as long as their is a sufficient substrate available the initial reaction increases linearly -if substrate is limited increase in enzyme concentration will not increase the reaction and substrate becomes a limiting factor
46
What is a competitive inhibitor
They only join to the active site -either some of it or all of it
47
What does a competitive inhibitor do?
-stops the substrate from bonding to the active site -can be reversible or irreversible -when the inhibitor leaves the substrate can bind again
48
What is a non-competitive inhibitor?
-bind to anywhere on the enzyme other than the active site
49
What does an non competitive inhibitor do ?
-cause conformational change of the active site -stops the substrate form being able to bind -irreversible or reversible
50
What is a reversible inhibitor called ?
-inhibitor
51
What is a irreversible inhibitor Called ?
-Inactivator
52
How do competitive inhibitors affect rate of reaction ?
-if substrate concentration is increased the change of the substrate binding to the actuve sitr -ROR increases as substrate concentration increases -both reach same plateau just takes longer with inhibitor
53
What is negative feedback ?
-mechanism in which a negative effect of homeostasis is reuturned to normal -some controlled by end-product inhibition
54
What is an end product inhibitor?
When the end product of a metabolic pathway becomes the inhibitor of the first part of that pathway
55
What does an end product inhibitor do m?
Stops the pathways from happening all the time and producing too much intermediate or end product
56
Examples of inhibitors
-ATPaze -ACE -Protease -nucleoside reverse transcriptase inhibitor

Biology (8 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions