Lecture 12: Enzyme kinetics, inhibition and regulation II Flashcards
What is Vo or Vi?
Is the initial rate / velocity (at time zero) at a particular substrate concentration
What are isoenzymes / isozymes?
- are different forms of a multi unit enzymes
- they differ in physical properties, kinetic properties and antigenic properties
- BUT they catalyse the SAME reaction
What are zymogens?
How are they activated?
How does proteolytic cleavage regulate enzymes?
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 are enzymes regulated?
- Allosteric effects
- Covalent modification
- Proteolytic cleavage
How does allosteric effects regulate enzymes?
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 does covalent modification regulate enzymes?
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