BCH210H1 Lecture Notes - Lecture 21: Protonation, Pyrimidine, Riboflavin
49
BCH210H1 Full Course Notes
Verified Note
49 documents
Document Summary
Mechanisms of enzymes: catalysis: mechanisms of specific enzymes, cofactors and coenzymes. Majority of enzymes does this --> also called covalent catalysis. Enzyme in active site would have residue with a lone pair of electrons that attack a phosphoryl group, a carbonyl group, etc. This attack results in a transition state which is unstable and bonds are changing. In the end, you have a leaving group since you are breaking a bond. Nucleophile attacks the leaving group directly opposite of it. Below show the stable intermediates --> represented as troughs on the diagram. You get the first transition state and you get the intermediate which is usually bonded covalently to the enzyme active site. The first transition state is always the rate limiting step. Have two substrates with the barrier and a stable intermediate being formed. First thing they do is the proximity effect which is bringing the reactants close together. This increases the likelihood of forming the stable intermediates.
