Enzymes as Biological Catalysts Flashcards

1
Q

What do enzymes do?

A

Speed up the rate at which a reaction reaches equilibrium

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

Do enzymes affect the position of equilibrium?

A

No

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

What are enzymes made of?

A

Mostly proteins but some types of RNA (ribozymes`) can also be catalysts

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

What conditions are optimal for enzymes?

A

Body temperature, aqueous solution and neutral pH

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

What is specificity in relation to proteins?

A

Each enzyme has a limited range of substrates. Some can distinguish stereoisomers

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

What is enzyme potency?

A

Each enzyme can convert many substrate molecules into product per second

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

What happens at a reaction’s transition state?

A

The reaction takes place really rapidly which is unstable for the reactants

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

How do enzymes affect the transition state?

A

They bind to the reactants and make it stable, also reducing the activation energy by providing alternative pathways

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

What is the transition state?

A

The reaction intermediate species which has the greatest free energy hence why it is unstable

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

What causes glycogen storage disease?

A

It is an enzyme deficiency that results in failure of glycogen to enter the transition ‘phosphorylated’ state and so there is defective glycogen synthesis/breakdown

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

What are the symptoms of glycogen storage disease?

A

Hypoglycaemia, hepatomegaly (liver swelling), skin and mouth ulcers, bacterial/fungal infection and bowel inflammation/irritability

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

What is the treatment for glycogen storage disease?

A

Slow release glucose meal and feeding little and often to mimic glycogen conversion to glucose

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

What is a cofactor?

A

Metal ions (inorganic) which many enzymes depend on for catalytic activity

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

What do cofactors form with enzymes?

A

Metal co-ordination centre in the enzyme - metalloprotein

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

What is a coenzyme?

A

An organic molecule which many enzymes depend on for catalytic activity

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

What do coenzymes do?

A

Mostly associate with the coenzyme transiently and change charge or structure during the reaction but are regenerated eg VITAMINS

17
Q

What are tightly bound coenzymes called?

A

Prosthetic groups

18
Q

What is an enzyme without a cofactor called?

19
Q

What is an enzyme with a cofactor called?

A

Holoenzyme = apoenzyme + cofactor

20
Q

What do cofactors do?

A

Stabilise transition states

21
Q

Where does the substrate bind in the enzyme?

A

Active site - a cleft or crevice that contains amino acids essential for catalytic activity for highly specific reactions

22
Q

What is the lock and key model?

A

Active site of the unbound enzyme is complementary to the shape of the substrate

23
Q

What is the induced fit model?

A

Binding of the substrate induces a conformational change in the enzyme resulting in complementary fit

24
Q

What are isozymes?

A

Isoforms of enzymes - they catalyse the same reaction but have different properties and structure

25
Where are isozymes synthesised?
During different stages of foetal and embryonic development
26
Where are isozymes present?
In different tissues and in different cellular locations
27
In lactate dehydrogenase what are the 2 subunits and what do they do?
H (heart) - promotes aerobic respiration | M (muscle) - promotes anaerobic respiration
28
What is the role of creatine kinase?
It is a dimeric protein which binds to the muscle sarcomere. M form is produced in skeletal muscle (MM), B form is produced in brain (BB) and the heart produces both types = heterodimer (MB). Brain type in blood suggests stroke/tumour, whilst heart type suggests heart attack.
29
What is the role of enzyme activation by phosphorylation?
Can convert enzymes to active or inactive forms by protein kinases - fast, reversible and found in all cells - especially in energy generation
30
What are zymogens?
Inactive precursors of an enzyme
31
What happens in irreversible covalent modification to regulate enzyme activity?
Results in activation of enzymes. Zymogens are irreversibly transformed into active enzymes by cleavage of a covalent bond
32
What are some examples of digestive enzymes?
Trypsin, chymotrypsin, carboxypeptidase A and B, elastase, pepsin and phospholipase
33
What are some examples of blood coagulation factors?
Factors VII, IX, X, XI, and XIII, kallikrein and thrombin
34
What are some examples of enzymes in blood clot dissolving?
Plasminogen, and plasminogen activator
35
What are some examples of enzymes involved in programmed development?
Chitin synthetase, cocoons and collagenase