BIBC 100 Study Guide - Final Guide: Serine Protease, Enzyme Catalysis, Catalytic Triad
Document Summary
Describe each mechanism by which enzymes decrease the activation energy for product formation (3 mechanisms) Describe the structure of chymotrypsin and the critical components of the active site. Explain the catalytic mechanism of chymotrypsin, including the 3 catalytic triad aa residues. Explain how substrate/transition state mimics are used as pharmaceuticals with examples. Explain abzymes and relationship between catalysis and specificity. Enzymes classified according to activity: oxidoreductases: transfer electrons, transferases: group transfer reactions, hydrolases: hydrolysis reactions, lyases: cleavage of c-c, c-o, or c-n bonds by elimination double bond/rings or addition of groups to double bonds. Isomerases: transfer of groups within molecules to yield isomeric forms: ligases: formation of c-c, c-s, c-o, or c-n bonds by condensation with cleavage of atp. Enzymes interact w/ substrate to catalyze product formation by lowering activation energy: s + e es ep e + p, es and ep are reaction intermediates, decrease in activation energy increases reaction rates.
