Km Measure of binding affinity (roughly) The lower the Km, the tighter the binding Vmax - PowerPoint PPT Presentation

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

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