Duration
15h Th
Number of credits
| Master in chemistry (120 ECTS) | 2 crédits | |||
| Master in chemistry (60 ECTS) | 2 crédits |
Lecturer
Language(s) of instruction
French language
Organisation and examination
Teaching in the second semester
Units courses prerequisite and corequisite
Prerequisite or corequisite units are presented within each program
Learning unit contents
Chapter 1: General properties of enzymes. Chapter 2: Steady-state kinetics. Chapter 3: Enzyme inhibition. Chapter 4: Effect of pH, temperature, viscosity and other experimental factors. Chapter 5: Reactions of two substrates. Chapter 6: Transient-state kinetics. Chapter 7: Cooperativity and allosteric interactions. Chapter 8: Enzyme inactivators. Chapter 9: Enzyme cofactors. Chapter 10: Mechanism of chymotrypsin. Chapter 11: Basic catalytic principles. Chapter 12: Regulation of catalytic activity.
Learning outcomes of the learning unit
The aim of the course is to make students familiar with both enzyme mechanisms and fundamentals of enzyme kinetics.
Prerequisite knowledge and skills
Biochemistry course (BAC3), which includes an introduction to enzyme catalysis (chapters 1-3).
Planned learning activities and teaching methods
Most lectures are given using the blackboard and (hopefuly) white chalk.
Mode of delivery (face-to-face ; distance-learning)
Face-to-face only
Recommended or required readings
Reference book: A. Cornish-Bowden, Fundamentals of enzyme kinetics, fourth edition, Wiley-Blackwell, 2012.
Assessment methods and criteria
Oral exam
Work placement(s)
Non applicable
Organizational remarks
The students will contact the professor asap in order to plan the course schedule
Contacts
André Matagne, PhD, Professor, Enzymology and Protein Folding, Centre for Protein Engineering, Life Science Department, Institut de Chimie B6c (room 3/1), Allée de la Chimie, 3, University of Liège, B4000 Liège (Sart-Tilman), Tel.: +32 (0)4 3663419, Fax: +32 (0)4 3663396, Email: amatagne@ulg.ac.be