BCMB20002 Lecture Notes - Lecture 10: Enzyme Catalysis, Zanamivir, Phenylpyruvic Acid
3 Aug 2018
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Document Summary
Enzymes are biomolecules (e. g. usually proteins) that have a distinctive 3-d structure and employ catalytic mechanisms such as weak interactions, acid-base, covalent & metal ion catalysis. Enzymes provide a specific environment, i. e. active site , for a given reaction to. The active sites of enzymes are lined with functional groups (usually from amino proceed rapidly compared to the uncatalysed or spontaneous reaction acids) that bind the substrate(s) and catalyze the chemical transformation to product(s) Enzymes affect reaction rates , but not equilibria: Enzymes lo er the activation energy required to convert a substrate(s) to product(s) and perform this function with a high degree of specificity. Enzyme catalyzed reactions are characterized by the formation of a complex between enzyme and substrate (es) Enzyme catalysis is formally described as the stabilization of the transition state through tight binding to the enzyme. (transition state = highly stabilised)
