III.2 Regulation

6 important questions on III.2 Regulation

How does regulation affect Km and Vmax?

Competitive inhibition: Km increases
Non-competitive inhibition: Vmax decreases
Mixed inhibition: Km increases, Vmax decreases

What are examples of irreversible inhibition?

  • Denaturation and/or digestion
  • Irreversible binding of agents
  • Modifications of primary structure

What is phosphorylation? What is responsible for it?

Phosphorylation can either activate of inactivate an enzyme. This can be direct of indirect.
Protein kinases are responsible for this kind of regulation.
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What is cooperativity? How is it achieved?

Cooperativity means that a complex changes its affinity when a ligand is bound to it.

What are the T and R state of an enzyme?

The T state has low ligand binding affinity. The R state has high binding affinity. This is the case for cooperative protein complexes that have two conformations.

What is allostery? What does an allosteric effector?

Allostery means that the activity of the protein itself changes in response to the binding of an effecter molecule.
An allosteric effector affects the equilibrium between the T and R state.

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