CHEM237 Lecture Notes - Lecture 14: Serine Protease, Enzyme Kinetics, Dissociation Constant
20 Jun 2017
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Document Summary
Enzyme: protein/rna catalyst for biochemical reactions that binds specifically to certain substrates to catalyze reactions under mild conditions (and are typically regulated by regulatory enzymes) Specificity: binding occurs with high (geometric) specificity to the complimentary structure at the active site. Rate is accelerated by increasing the concentration of reactants, adding reactive groups, stabilizing the transition state, and orienting the reactants, active site is complementary to the ts. Cofactors: small molecules that provide additional reactive groups for catalysis (nad+, nadh - redox, biotin - decarboxylation, riboflavin- redox) Enzymes have specificity pockets that match up with the substrate (e. g. : donor to acceptor for h bonds, negative to positive for ionic interactions, complimentary hydrophobic patches) Carbohydrates have a lot of oh groups so enzymes that would catalyze will form h bonds. Ts stabilization happens between es e+p (bigger 2nd bump), es is the bottom between the 2 bumps (assumes ea is the same regardless of whether catalyzed)
