Lecture 12: Enzyme kinetics, inhibition and regulation II Flashcards

1
Q

What is Vo or Vi?

A

Is the initial rate / velocity (at time zero) at a particular substrate concentration

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

What are isoenzymes / isozymes?

A
  • are different forms of a multi unit enzymes
  • they differ in physical properties, kinetic properties and antigenic properties
  • BUT they catalyse the SAME reaction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are zymogens?

How are they activated?

How does proteolytic cleavage regulate enzymes?

A

Zymogens are inactive forms of enzymes
Zymogens are activated by the cleavage of proteases to the zymogen polypeptide which removes a peptide/peptides to activate to the enzyme
- proteolytic cleavage activates zymogens

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

How are enzymes regulated?

A
  1. Allosteric effects
  2. Covalent modification
  3. Proteolytic cleavage
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

How does allosteric effects regulate enzymes?

A

Activity can be regulated by binding of molecules away from the active site, which can inhibit or activate the enzyme
- These regulatory effects are achieved by conformation change in the protein when the effector molecule binds

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

How does covalent modification regulate enzymes?

A

Is is the addition of molecule / group which changes its activity.

  • are mostly reversible
  • Phosphorylation/dephosphorylation involving sides chains of Ser, Thr or Tyr (R-OH)
  • Enzymes involved are protein kinases and phosphates
How well did you know this?
1
Not at all
2
3
4
5
Perfectly