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Understanding Enzyme Kinetics: Michaelis-Menten and Inhibition Mechanisms in Chemical Reaction Engineering

This lecture delves into the field of Chemical Reaction Engineering, focusing on enzyme kinetics, specifically Michaelis-Menten dynamics, and the inhibition types affecting enzyme activity. We explore enzyme function, turnover rates, and derive key equations including the Michaelis-Menten and Lineweaver-Burk plots. The lecture covers competitive, uncompetitive, and non-competitive inhibition mechanisms that influence reaction rates. Understanding these concepts is key for designing efficient biochemical reactors and optimizing industrial processes involving enzymes.

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Understanding Enzyme Kinetics: Michaelis-Menten and Inhibition Mechanisms in Chemical Reaction Engineering

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  1. Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they take place.

  2. Today’slecture • Enzymes • Michealis-Menten Kinetics • Lineweaver-Burk Plot • Enzyme Inhibition • Competitive • Uncompetitive

  3. Last lecture

  4. Last lecture

  5. Enzymes Michaelis-Menten Kinetics. Enzymes are protein like substances with catalytic properties. Enzymeunease. [From Biochemistry, 3/E by Stryer, copywrited 1988 by LubertStryer. Used with permission of W.H. Freeman and Company.]

  6. Enzymes It provides a pathway for the substrate to proceed at a faster rate. The substrate, S, reacts to form a product P. Slow S P Fast A given enzyme can only catalyze only one reaction. Example, Urea is decomposed by the enzyme urease.

  7. A given enzymecanonlycatalyzeonlyonereaction. Urea is decomposed by the enzymeurease, as shownbelow.

  8. The correspondingmechanism is:

  9. Michaelis-Menten Kinetics

  10. Michaelis-MentenKinetics

  11. Vmax=kcat* Et Turnover Number: kcat Number of substrate molecules (moles) converted to product in a given time (s) on a single enzyme molecule (molecules/molecule/time) For the reaction kcat H2O2 + E →H2O + O + E 40,000,000 molecules of H2O2 converted to product per second on a single enzyme molecule.

  12. Summary

  13. (Michaelis-Menten plot) Vmax Solving: KM=S1/2 therefore KMis the concentration at which the rate is half the maximum rate -rs Michaelis-Menten Equation S1/2 CS

  14. Invertingyields Lineweaver-BurkPlot 1/-rS slope = KM/Vmax 1/Vmax 1/S

  15. Types of Enzyme Inhibition Competitive Uncompetitive Non-competitive

  16. Competitive Inhibition

  17. CompetitiveInhibition 1) Mechanisms:

  18. CompetitiveInhibition • 2) Rates:

  19. CompetitiveInhibition

  20. CompetitiveInhibition From before (no competition): Competitive No Inhibition Increasing CI Competitive Intercept does not change, slope increases as inhibitor concentration increases

  21. Uncompetitive Inhibition Inhibition only has affinity for enzyme-substrate complex Developing the rate law (1) (2)

  22. Adding (1) and (2) From (2)

  23. Total enzyme

  24. Slope remains the same but intercept changes as inhibitor concentration is increased Lineweaver-Burk Plot for uncompetitive inhibition

  25. Noncompetitive Inhibition (Mixed) E + S E·S P + E (inactive)I.E+ S I.E.S (inactive) Increasing I +I -I -I +I No Inhibition Both slope and intercept changes

  26. End of Lecture 15

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