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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. - PowerPoint PPT Presentation
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• 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?
Double-reciprocal plot(Lineweaver-Burk)
Problems 7a-d,8a,b
Regulation
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
Competitive inhibition
Noncompetitive inhibition
Regulation
Reversible– Substrate level regulation – Competitive inhibitors– Noncompetitive inhibitors– Allosteric regulation (activators and
inhibitors) – Covalent modification (reversible)– Proteolytic cleavage
Reversible covalent modification
Phosphorylation
Dephosphorylation
Proteolytic cleavage
Only extracellular
Metabolism
Energy flow in cells