Duration
15h Th, 10h SEM
Number of credits
| Master in chemistry, research focus | 3 crédits | |||
| Master in chemistry, teaching focus (Réinscription uniquement, pas de nouvelle inscription) | 3 crédits | |||
| Master in chemistry, professional focus | 3 crédits |
Lecturer
Language(s) of instruction
French language
Organisation and examination
Teaching in the second semester
Schedule
Units courses prerequisite and corequisite
Prerequisite or corequisite units are presented within each program
Learning unit contents
This course is organized into twelve chapters: Chapter 1: General properties of enzymes. Chapter 2: Enzyme kinetics: steady-state kinetics and independent sites. Chapter 3: Enzyme inhibition. Chapter 4: Effect of physicochemical parameters. Chapter 5: Two-substrate systems. Chapter 6: Transient-state kinetics. Chapter 7: Cooperativity and allosteric interactions. Chapter 8: Enzyme inactivators. Chapter 9: Enzyme cofactors. Chapter 10: Mechanism of action of chymotrypsin. Chapter 11: Basic catalytic principles. Chapter 12: Regulation of catalytic activity.
Learning outcomes of the learning unit
By the end of this course, students will understand the fundamental principles of enzyme function, catalysis, and regulation. They will have acquired the concepts of enzyme kinetics required to characterize enzyme activity.
Prerequisite knowledge and skills
Students are expected to have completed the bachelor's-level course in chemistry entitled "Biochemistry", in which the topics covered in Chapters 1-3 of the present course were introduced through lectures and tutorial exercises.
Planned learning activities and teaching methods
Teaching is primarily based on independent study of the course notes. No regular lectures are scheduled. The study of the different chapters may be organized on a weekly basis. After studying each chapter, students may request a meeting with the professor to obtain further explanations and discuss any points they find difficult. These meetings may also be held weekly, depending on the students' needs.
Mode of delivery (face to face, distance learning, hybrid learning)
Face-to-face course
Further information:
Supervised independent study, supplemented, at the students' request, by face-to-face meetings with the professor.
Course materials and recommended or required readings
Lecture notes will be available.
Reference book:
A. Cornish-Bowden, Fundamentals of enzyme kinetics, fourth edition, Wiley-Blackwell, 2012.
A.R. Fersht, Structure and mechanism in protein science, W.H. Freeman and Co, 1999.
Exam(s) in session
Any session
- In-person
oral exam
Additional information:
The evaluation will be made on the basis of an oral presentation relating to the analysis of a few articles.
Work placement(s)
Non applicable
Organisational remarks and main changes to the course
Students are responsible for contacting the professor at the beginning of the semester to obtain the course materials and agree on the practical organization of the course, including the weekly schedule for studying the chapters and any discussion sessions.
Contacts
André Matagne, PhD, Full Professor, Enzymology and Protein Folding, Centre for Protein Engineering, Life Science Department, Institut de Chimie B6c (room 3/1), Quartier Agora, Allée du 6 Août, 13, University of Liège, B4000 Liège (Sart-Tilman), Tel.: +32 (0)4 3663419, Email: amatagne@ulg.ac.be