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

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
How many substrate level phosphorylation are there in glycolysis
4
26
Why is controlling glycolysis important
To link supple of atp with demand or if needed for storage To allow cells to respond to the environment
27
Which type of enzymes are used to control catabolic reactions
Rate limiting enzymes (slow rate of reactions)
28
How do you limit rate of enzymes (4 ways)
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
How is enzyme access to substrate limited
Via compartmentalisation Either substrate or enzyme stick to one area
30
Which 3 enzymes are controlled in glycolysis
Hexokinase Phosphofructo kinase Pyruvate kinase
31
How is hexokinase inactivated when too much Glucose 6 phosphate is present
Allosterically inactivated via negative feedback
32
Why is glucose 6 phosphate important
Because it is used as a glycogen store important for muscles etc
33
What allows phosphofructokinase activity (turning fructose 1 phosphate into fructose 1,6 bisphosphate)
Low ATP/energy levels Adenylate cyclase production of AMP activates the phosphofructokinase
34
Which 3 things in too much presence stops phosphofructokinase
ATP (not needed anymore) Low ph indicating too much lactate produced by pyruvate Citrate increase in the Krebs cycle
35
How is pyruvate kinase action increased (phosphoenolpyruvate into pyruvate)
The accumulation of fructose 1 6 bisphosphate in the investment stage of glycolysis causes activation of pyruvate kinase
36
How does fructose 2 6 bisphosphate presence allow for activation of phosphofructokinase
It decrease PFK affinity for atp and citrate which decrease its activity