Lecture 7 Flashcards

(14 cards)

1
Q

Energy charge

A

Large changes in ATP is not desirable. Aim is to keep ATP at 5mM. There are instant reserves of compounds able to do substrate level phosphorylation. But, only a few seconds supply.

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

Creatine Phosphate

A

Sprinting for 5 seconds (used for energy). Able to pass P -> ADP (substrate level)

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

1-3 bisphosphateglycerate

A

2nd half of glycolysis (3C sugar phosphate + phosphate)

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

Phosphoenolpyruvate

A

2nd half of glycolysis.

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

More instant ATP

A

Adenylate kinase can take 2 ADPs to make ATP and AMP. Increase AMP = decrease energy charge in cells.

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

Enzymatic control

A

Only one or two enzymes in a pathway regulate the flow. The slowest enzyme in the pathway determines overall speed. Rate limiting step.

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

Enzyme kinetics

A

At high [substrate], minor changes [substrate] will not affect the rate of reaction. Doubling or halving [substrate] isn’t even going to affect the rate. when [substrate] approaches Km, rate of reaction may increase or decrease.

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

Properties of rate limiting step

A

Irreversible. Committed step i.e cannot go back without other enzyme. Saturated with substrate. A low Km reflects high affinity for the substrate or, the substrate concentration is much higher than Km, so the enzyme works near Vmax.

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

Changing the flux

A
  1. making the limiting enzyme faster or slower
  2. Turn the rate limiting enzyme on/off or make it work the other way
  3. Increase rate of transcription/translation of the RLS or change rate of degradation.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

RLFs in catabolism

A

The rate limiting step is going to change under different circumstances e.g fed, fast, exercising, nutrients consumed and hormone control. Overriding =cofactor availability and [AMP] which is determined by ATP demand.

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

Phosphofructokinase

A

key regulatory enzyme in glycolysis. It is allosterically inhibited by high concentrations of its substrate, ATP, indicating that the cell has sufficient energy. PFK also has allosteric binding sites for AMP, which acts as an activator. When AMP binds, it signals that the cell needs more energy and promoting glycolysis. Additionally, high concentrations of citrate also inhibit PFK. Buildup of acetyl-CoA and other Krebs cycle intermediates, suggesting that energy production is already high. Citrate can diffuse into the cytoplasm and signal PFK to slow down glycolysis, preventing excess glucose breakdown.

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

Hexokinase: Feedback inhibition

A

Initial glucose trapping reaction. Inhibition by the product, G6P prevents excessive trapping and ATP wastage allowing the glucose to exit the cell. So if G6P us not being used, glucose is not trapped.

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

PDH-covalent modification

A

Inactivated by phosphorylation. Covalent attachment of phosphate which is catalysed by PDH kinase. Total amount of enzyme doesn’t change, just the ratio of phosphorylated to dephosphorylated. Reactivation by phosphatase causes phosphate release. PDH activity a valance between kinase and phosphatase.

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

futile cycle

A

When anabolic and catabolic reaction occurs at the same time e.g FA synthesis and
B O2.

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