Glycolysis And Control Flashcards

1
Q

What is glycolysis and what is the pathway called

A

Splitting of glucose into pyruvate x 2

The EMBDEN MAYERHOF PARNAS PATHWAY

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2
Q

Why is glycolysis important

A

Only source of energy in anaerobic respiration

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3
Q

Name the 3 stages of glycolysis

A

Investment

Splitting

Energy yield

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4
Q

How many ATP molecules are used / hydrolysed in investment and how many gained

A

2

4 are gained

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5
Q

What first happens to glucose and which enzyme is involved

A

Glucose is phosphorylated

Glucose 6 phosphate produced

Hexokinase enzyme uses atp hydrolysis to phosphorylate glucose

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6
Q

Why is it important for cells that glucose is phosphorylated

A

Phosphate is negatively charged which stops glucose leaking out of cells as much

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7
Q

What ion does hexokinase need and also any other enzyme to phosphorylate glucose etc

A

Mg++

Needed to stop the other 2 phosphates being hydrolysed (only 1 phosphate added)

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8
Q

Why is hexokinase better than glucokinase in phosphorylation of molecules like glucose

A

Because gluco kinase has a higher KM which means lower affinity to the molecules than hexokinase

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9
Q

Which carbon is phopshorylated on glucose by hexokinase atp hydrolysis

A

6 C

Forms CH2OPO3-

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10
Q

What happens to glucose 6 phosphate when produced by hexokinase

A

Isomerisation (change in structure)

Into fructose 6 phosphate

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11
Q

Explain the steps of how aldose sugar glucose 6 P turns into a ketose sugar fructose 6 P

A

The ring opens to form an exposed aldehyde group ( h c=o h)

This isn’t stable so forms an internal ester with C2OH

This forms a ketone

Then the C2 double O forms internal bond with another O

The ring closes to form a furanose 5C sugar

= fructose 6 phosphate (6c is phosphorylated)

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12
Q

What happens to fructose 1 phosphate (5c ring) after isomerisation

A

Phospho fructo kinase will phosphorylate C1 aswell as C6 (using atp hydrolysis and mg++)

Forms a fructose 1, 6 bisphosphate

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13
Q

Why does fructose 1 6 bisphosphate split into 2 x 3c molecules instead of being a furanose 5c ring

A

Because of the symmetry and the 2 negative charges on phosphates cause repulsion

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14
Q

What happens in splitting (include the 2 enzymes involved)

A
Fructose 1 6 bisphosphate (6c) is split into 
Dihydroxyacetone phosphate (x2) 

BY ALDOSE ENZYME

this then converts to glyceraldahyde 3 phosphate (x2) 3C

This is done using triose phosphate isomerase

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15
Q

Which enzyme converts dihydroxyacetone phosphate 3C into glyceraldahyde 3 phosphate

A

Triose phosphate isomerase

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16
Q

What is the gain of ATP in the energy yield stage of glycolysis

A

2 for each glyceraldahyde 3 phosphate (x2) = 4

17
Q

What is the first step in energy yield converting glyceraldahyde 3 phosphate

A

Glucose 3 phosphate dehydrogenase Enzyme

Allows conversion of NAD to NADH which oxidises(H removed from G3p)

G3p also gains a free phosphate to form

1,3 bisphosphoglycerate

18
Q

Where are the phosphates located on 1,3 bisphoshoglycerate converted from G3P

A

C1 and C3

19
Q

What is 1,3 bisphosphoglycerate converted to and how

A

3 phoshpoglycerate

Converted by removing a phosphate which binds to ADP to form a new ATP molecules (substrate level phosphorylation)

20
Q

Which enzyme dephosphorylates 1,3 bisphosglycerate to form a new ATP molecule

A

Phosphoglycerate kinase

21
Q

How does 3 phosphoglycerate turn into 2 phosphoglycerate

A

Phosphoglycerate mutase converts the PO group from C3 to C2 (central C)

22
Q

What happens to 2 phosphoglycerate produced by phosphoglycerate mutase enzyme

A

It is converted to phosphoenolpyruvate

H2O is removed from it by enolase enzyme

23
Q

Why is h20 removed from 2 phosphoglycerate

A

Increases energy production by adding another double bond

24
Q

Which enzyme dephosphorylates phosphoenolpyruvate to produce ATP and pyruvate

A

Pyruvate kinase

25
Q

How many substrate level phosphorylation are there in glycolysis

A

4

26
Q

Why is controlling glycolysis important

A

To link supple of atp with demand or if needed for storage

To allow cells to respond to the environment

27
Q

Which type of enzymes are used to control catabolic reactions

A

Rate limiting enzymes (slow rate of reactions)

28
Q

How do you limit rate of enzymes (4 ways)

A

1- control amount of enzyme

2- allosteric inactivation of the enzyme

3- covalent modification via kinase or phosphatase

4- controlling enzymes access to substrate

29
Q

How is enzyme access to substrate limited

A

Via compartmentalisation

Either substrate or enzyme stick to one area

30
Q

Which 3 enzymes are controlled in glycolysis

A

Hexokinase

Phosphofructo kinase

Pyruvate kinase

31
Q

How is hexokinase inactivated when too much Glucose 6 phosphate is present

A

Allosterically inactivated via negative feedback

32
Q

Why is glucose 6 phosphate important

A

Because it is used as a glycogen store important for muscles etc

33
Q

What allows phosphofructokinase activity (turning fructose 1 phosphate into fructose 1,6 bisphosphate)

A

Low ATP/energy levels

Adenylate cyclase production of AMP activates the phosphofructokinase

34
Q

Which 3 things in too much presence stops phosphofructokinase

A

ATP (not needed anymore)

Low ph indicating too much lactate produced by pyruvate

Citrate increase in the Krebs cycle

35
Q

How is pyruvate kinase action increased (phosphoenolpyruvate into pyruvate)

A

The accumulation of fructose 1 6 bisphosphate in the investment stage of glycolysis causes activation of pyruvate kinase

36
Q

How does fructose 2 6 bisphosphate presence allow for activation of phosphofructokinase

A

It decrease PFK affinity for atp and citrate which decrease its activity