| Code |
9117
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| Year |
3
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| Semester |
S2
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| ECTS Credits |
6
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| Workload |
PL(30H)/T(30H)
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| Scientific area |
Bioengenharia
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Mode of delivery |
face-to-face
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Work placements |
NA
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Learning outcomes |
It is intended that the student knows the basics of Enzymology. He should:
- Acquire notions of structure and general properties of enzymes.
- Understand general mechanisms of enzymatic action.
- Understand and apply concepts of enzyme kinetics.
- Know practical applications of enzymes.
At the end of the course the student should be able to:
- Classify and assign the systematic name to a particular enzyme.
- Relate the structure of enzymes with their catalytic function.
- Explain the physical and chemical processes by which enzymes produce catalysis.
- Propose a kinetic mechanism to explain the enzymatic action and deduce the rate equation of the enzymatic reaction in a situation of steady state.
- Identify different types of enzyme inhibitors and activators.
- Determine the initial rate of an enzymatic reaction.
- Perform experimentally the kinetic study of an enzyme in the absence or in presence of different inhibitors.
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Syllabus |
Theoretical classes:
1. Historic perspective.
2. General properties and nomenclature of enzymes.
3. Enzyme structure.
4. Thermodynamic aspects of mechanisms of enzymatic catalysis.
5. Enzyme mechanisms.
6. Kinetics of enzymatic reactions.
6.1. The mechanism of Michaelis and Menten. The steady state hypothesis.
6.2. Analysis of the Michaelis-Menten equation and methods for the determination of its kinetic parameters.
6.3. Reversible reactions.
6.4. Analysis of reaction progress curve.
7. Practical aspects when carrying out kinetic studies.
8. Methods for deduction of steady state rate equations.
9. Enzyme inhibition and activation.
10. Multisubstrate reactions.
11. Practical applications of enzymes.
Practical classes:
Implementation and discussion of two experimental studies (8h each): "Determination of the kinetic parameters of beta-glucosidase" and "Kinetic study of alkaline phosphatase: actions of different types of inhibitors."
Solving of exercises.
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Main Bibliography |
Required reading:
• A. Cornish-Bowden (2012) – Fundamentals of Enzyme Kinetics. 4th ed. Wiley-Blackwell.
• T. Palmer (1995) – Understanding Enzymes. 4th ed. Prentice Hall/Ellis Horwood.
• A. Fersht (1998) – Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding. W.H. Freeman and Company.
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Language |
Portuguese. Tutorial support is available in English.
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