Metabolism Overview Flashcards

1
Q

What is catabolism?

A

Metabolic breakdown of complex substances into smaller products

(Food –> building blocks + energy + heat)

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

What is anabolism?

A

Energy-requiring transformation of simpler substances into more complex ones

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

Why are substances broken down step-wise rather than all in one go?

A

Step-wise releases small, usable packages of energy

Each step has a smaller activation energy (all in one go = lots of energy wasted as heat and high Ea)

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

Why are forward and reverse pathways not direct opposites of each other?

A

Allows separate regulation

Prevents ‘futile cycle’

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

What is another term for activated carrier molecules?

A

Cofactors

Coenzymes

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

Why is energy stored at each step of an energetically favourable reaction?

A

To be used in energetically unfavourable reactions

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

What bonds in ATP are broken to release energy?

A

Phosphoanhydride

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

What properties make ATP suitable for energy storage in humans?

A

Chemically stable at physiological pH (6-9)

Structural features can be recognised by specific proteins, enzymes, etc

Hydrolysis releases energy

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

What does ΔG mean?

A

Change in free energy

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

What does it mean when ΔG is negative?

A

Energy released

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

What is the ΔG of ATP hydrolysis?

A

-31 to -50kJ/mol

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

Why is ATP hydrolysis energetically favourable?

A

Relieves electrostatic repulsion between phosphate groups (unstable molecule)

Released phosphate ion is resonance stabilised (electron delocalisation)

Increase in entropy

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

How much energy is release when ATP is hydrolysed to AMP + PPi?

A

Almost twice as much as ATP to ADP hydrolysis

As PPi spontaneously breaks down into two Pi

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

What is PPi called?

A

Pyrophosphate

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

Give some of the functions of ATP

A

Cell motility and muscle contraction

Active transport

Metabolic control by regulating enzyme activity

Activate/phosphorylate molecules

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

What UTP used for?

A

Synthesis of complex sugars

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

What is GTP used for?

A

Protein synthesis (translation)

Microtubule elongation

18
Q

Which activated energy carriers carry electrons and protons?

A

NAD(H)

NADP(H)

FAD(H2)

19
Q

What does acetyl coenzyme A carry?

20
Q

Which activated energy carrier carries a carboxyl group?

A

Carboxylated biotin

21
Q

What activated energy carrier carries a methyl group?

A

S-adenosylmethionine

22
Q

What activated energy carrier carries a glucose?

A

Uridine diphosphate glucose (UDP-glucose)

23
Q

What does NAD stand for?

A

Nicotinamide adenine dinucleotide

24
Q

What are the main differences between NAD+ and NADP+?

A

NADP+ has a phosphate group

NADP+ replaces NAD+ in anabolic reactions

25
What happens molecularly when NAD+ is reduced?
Nicotinamide group accepts one H and an electron (leaving a spare proton)
26
What does FAD stand for?
Flavin adenine dinucleotide
27
What happens molecularly when FAD is reduced?
Flavin group accepts two H (added to nitrogens) | Originally neutral so no spare protons
28
What type of bonds does coenzyme A form with carboxylic acids?
Thioester
29
How do we write the structure of coenzyme A?
CoA-SH
30
What are the three main stages of catabolism of sugars, fats and amino acids?
Conversion to acetyl unit Krebs/TCA cycle Oxidative phosphorylation
31
What is pyruvate converted to in anaerobic respiration?
Lactate/lactic acid
32
What is the structure of pyruvate?
-OOC--CO--CH3
33
What enzyme catalyses anaerobic respiration?
Lactate dehydrogenase
34
What is the purpose of anaerobic respiration?
Regenerate NAD+ so glycolysis can continue
35
By what process is glucose converted to the acetyl unit?
Glycolysis
36
By what process is a fatty acid converted to the acetyl unit?
Beta oxidation
37
How is an amino acid converted to the acetyl unit?
Transamination
38
How can regulation of metabolic pathways be achieved?
Changes in amount of enzyme (gene expression) Changes in enzyme activity
39
How can enzyme activity be altered?
Allosteric regulation/binding of allosteric regulators Phosphorylation and dephosphorylation
40
What kind of alteration to enzyme activity is instantaneous and local?
Allosteric regulation