Protein Regulation Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What is allosteric regulation?

A

When external substances, such as substrate can prompt changes of an enzyme between a high affinity T state and a low affinity R state.

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

What are the two enzymes involved in the phosphorylation of proteins?

A

Protein kinases: transfer terminal phosphate of ATP to a protein.
Protein phosphotases: reverse effects of kinases, which the hydrolytic removal of a phosphate group.

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

How is proteolytic cleavage of proteins regulated?

A

Endogenous activators such as pancreatic trypsin inhibitor

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

What is a zymogen?

A

An inactive precursor to a hormone which can be activated by proteolytic cleavage.

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

What are the activators and inhibitors of phosphofructokinase?

A

Activators: AMP, fructose 2,6 bisphosphate
Inhibitors: ATP, citrate, h+

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

What is an enzyme cascade?

A

When enzymes activate molecules, one after the other and the number of molecules increases geometrically.

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

What is the enzyme activated at the end of the blood clotting cascade (and from what inactive precusor is it activated)?

A

Thrombin (activated from prothrombin)

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

What are the short term methods of regulating hormones?

A

Allosteric regulation, regulation by substrate and product concentration, as well as covalent modification.

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

How is trypsin activated?

A

Edniopeptidase cataysles the production of trypsinogen to trypsin.

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

What enzymes is trypsin involved in the activation of?

A

Activation of various spzymogens by protolytic cleavage, Chymotrypsinpgen to pie- chymotrpsin, proelastase to elastase, procarboxypeptidase to carboxypepetidase, prolipase to lipase

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

What is the action of thrombon at the end of the blood clotting cascade?

A

Cataylses the formation of fibrin from firbogen, protelyticaly cleaving n linked negatively charged peptidases allowing fibrin molecules to cross linked with one another.

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

What is an endgoenous inhibitor?

A

Inhibits protease activity.

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

What is an example of an endogenous inhibitor and how is it clinically relevant?

A

A1 antitrypsin, a 53 kda plasma protein which inhibits protases, and there is a deficiency in this in emphysema, so elastase digest the walls of the lungs.

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

What clotting factor is missing in Haemophilia?

A

VIII

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

How is blood clotting localised?

A

Calcium ions attach to receptors on damaged endothelial linings, and prothrombin attaches to this at the site of injury, which helps transform fibrogen into fibrinogen.

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

How does blood clot?

A

Thrombin cataysles the removal of firbopeptides a and b from fibrinogen to form fibrin, and the exposed n terminal ends can now make amide bonds with the exposed c terminal ends, and the bonds connect to form a fibrin mesh across a wound.