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1. Introduction to biochemistry
- Prof. Gerald W. Feigenson
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2. Amino acids and peptides
- Prof. Gerald W. Feigenson
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3. Protein structure principles
- Prof. Gerald W. Feigenson
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4. Observed protein structures
- Prof. Gerald W. Feigenson
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5. Protein folds and IV structure
- Prof. Gerald W. Feigenson
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6. Protein stability and folding
- Prof. Gerald W. Feigenson
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7. Haemoglobin structure and stability
- Prof. Gerald W. Feigenson
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8. Enzyme specificity and catalysis
- Prof. Gerald W. Feigenson
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9. Enzyme kinetics (Michaelis-Menten)
- Prof. Gerald W. Feigenson
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10. Enzyme inhibition; chymotrypsin
- Prof. Gerald W. Feigenson
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11. Enzyme regulation and coenzymes
- Prof. Gerald W. Feigenson
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12. Lipids, biomembranes and membrane proteins
- Prof. Gerald W. Feigenson
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13. Structure and function of carbohydrates
- Prof. Gerald W. Feigenson
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14. Metabolism principles
- Prof. Gerald W. Feigenson
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15. Glycolysis - energy and useful cell chemicals
- Prof. Gerald W. Feigenson
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16. Glycolysis control
- Prof. Gerald W. Feigenson
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17. Metabolism of pyruvate and fat
- Prof. Gerald W. Feigenson
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18. Urea cycle; oxidative phosphorylation 1
- Prof. Gerald W. Feigenson
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19. Urea cycle; oxidative phosphorylation 2
- Prof. Gerald W. Feigenson
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20. Light-driven reactions in photosynthesis
- Prof. Gerald W. Feigenson
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21. Gluconeogenesis and the Calvin cycle
- Prof. Gerald W. Feigenson
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22. Synthesis of lipids and N-containing molecules 1
- Prof. Gerald W. Feigenson
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23. Synthesis of lipids and N-containing molecules 2
- Prof. Gerald W. Feigenson
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24. Hormone mechanisms
- Prof. Gerald W. Feigenson
Printable Handouts
Navigable Slide Index
- Introduction
- Lecture outline
- Summary of how catalysts work
- Principles of kinetics
- Comparing two kinetic 'thought experiments'
- How enzymes work
- Enzyme kinetics: a simple, useful equation
- Useful features of the Michaelis-Menten Equation
- Meaning of Km
- Complexity: more than one product
- Complexity: more than one substrate
- How to measure KM and VMAX
- The Lineweaver-Burk plot, I/V vs. 1/[S]
- Using the Lineweaver-Burk plot
- Lecture summary
Topics Covered
- Initial reaction velocity
- Catalysed vs. uncatalysed reaction pathways
- Enzyme saturation/Maximum reaction velocity
- Michaelis-Menten equation
- Energy barriers and rate constants
- Measuring Km and Vmax
- The Lineweaver-Burk plot
Talk Citation
Feigenson, G.W. (2022, November 27). Enzyme kinetics (Michaelis-Menten) [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 3, 2024, from https://doi.org/10.69645/JFTX7058.Export Citation (RIS)
Publication History
Financial Disclosures
- Gerald Feigenson has no commercial/financial relationships to disclose.
Request access to the Principles of Biochemistry lecture series, an extensive introductory to the field of biochemistry. An HSTalks representative will contact you with more information about this series and getting unrestricted access to it.
A selection of talks on Biochemistry
Transcript
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0:00
Hello. Welcome to this Principles of Biochemistry lecture series.
I'm Jerry Feigenson, a professor in
the Department of Molecular Biology and Genetics at Cornell University in the USA.
In the eighth lecture,
you learned about different types of enzymes and some principles of enzyme kinetics.
And you saw that enzyme catalysts work by two different principles,
binding to and stabilizing the transition state and forcing
the mechanism to follow a pathway that has a lower transition state free energy.
0:43
In this ninth lecture,
you will learn how useful is the concept of initial reaction velocity.
And you will see that plotting initial reaction velocity versus substrate concentration
shows a big difference between catalyzed and uncatalyzed reactions.
You will see the usefulness of what is called Michaelis-Menten kinetics.
We'll see pre-energy barriers at every step along the reaction pathway.
And we will see the usefulness of
the double-reciprocal or Lineweaver-Burk plot to find kinetic parameters.
1:25
Just to remind you,
before we start talking more about catalysis,
let me summarize how catalysts work.
Only two ways: first,
whatever is the transition state,
the enzyme will bind to it and stabilize it,
thereby lowering its free energy.
Or whatever is the uncatalyzed reaction mechanism,
the enzyme will change it.
The enzyme will force a new reaction path that has a lower free energy transition state.