KIN217 Chapter Notes - Chapter 8: Oxyanion Hole, Methionine, Tryptophan
Document Summary
Chapter 8 mechanisms and inhibitors allosteric enzymes are not only catalysts but are also information sensors. 8. 1 a few basic catalytic strategies are used by many enzymes all enzymes operate by facilitating the formation of the transition state. How transition state is formed varies from enzyme to enzyme but most commonly employ one or more of the following strategies: Covalent catalysis active site contains a reactive group (nucleophile) that becomes temporarily covalently modified. Nucleophile attracted to regions of positive charge in another molecule. Electrophile receive electrons from nucleophile; initially electron deficient. General acid-base catalysis molecule other than water plays role of proton donor or acceptor. Metal ion catalysis number of ways. Electrophilic catalyst stabilize negative charge on a rxn intermediate. Generate nucleophile by increasing acidity of nearby molecule. Bind to substrate, increasing # of interactions b/w enzyme and thus increasing the binding energy. Serve role of cofactors for many enzymes.