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Km Measure of binding affinity (roughly) The lower the Km, the tighter the binding Vmax

Km Measure of binding affinity (roughly) The lower the Km, the tighter the binding Vmax Maximum rate of enzyme Determined by turnover number (k cat ). How best to calculate them?. Double-reciprocal plot (Lineweaver-Burk). Problems 7a-d,8a,b. Regulation. Regulation.

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Km Measure of binding affinity (roughly) The lower the Km, the tighter the binding Vmax

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  1. Km • Measure of binding affinity (roughly) • The lower the Km, the tighter the binding • Vmax • Maximum rate of enzyme • Determined by turnover number (kcat) How best to calculate them?

  2. Double-reciprocal plot(Lineweaver-Burk)

  3. Problems 7a-d,8a,b

  4. Regulation

  5. Regulation • Irreversible inhibitors—generally not natural part of cell • Drugs and toxins • Covalent modification • Aspirin • Reversible • Substrate level regulation • Competitive inhibitors • Noncompetitive inhibitors • Allosteric regulation (activators and inhibitors) • Covalent modification (reversible) • Proteolytic cleavage

  6. Competitive inhibition

  7. Noncompetitive inhibition

  8. Regulation Reversible • Substrate level regulation • Competitive inhibitors • Noncompetitive inhibitors • Allosteric regulation (activators and inhibitors) • Covalent modification (reversible) • Proteolytic cleavage

  9. Reversible covalent modification Phosphorylation Dephosphorylation

  10. Proteolytic cleavage Only extracellular

  11. Metabolism Energy flow in cells

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