This course aims to describe the molecular basis of biocatalysis. The chemistry of enzymatic reactions is approached from all angles: kinetic, thermodynamic, mechanistic and supramolecular.
1) Make a link beween chemical and enzymatic catlyses
2) Define the main inhibition modes of enzymes.
3) Give some examples of detailed enzymatic mechanisms.
4) Understanding the transfer of chirality from an enzyme to its ligands.
Based on historical discoveries, this course first introduces the basic concepts of molecular recognition (Emil Fischer), stereochemistry of natural molecules (Louis Pasteur) and energy profiles of biocatalyzed reactions (Linus Pauling). The mechanisms and biological functions of hydrolases are then developed. The rational design of inhibitors and the use of enzymes in organic synthesis are also illustrated. Asymmetric biocatalysis by lipases is also detailed. An introduction to directed enzyme evolution concludes this course.
An oral examination assesses the students' knowledge.
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