Enzymes: Catalytic Strategies

This lecture covers the catalytic strategies employed by enzymes, focusing on proteases and carbonic anhydrase. It explains the mechanisms of proteases in cleaving peptide bonds and the stabilization of transition states. The lecture also delves into the specificity of chymotrypsin and trypsin, as well as the catalytic mechanism of carbonic anhydrase. Different classes of proteases, such as aspartyl proteases and metalloproteases, are discussed. The role of pH in catalysis and the catalytic mechanisms of serine proteases are explored. The lecture concludes with an overview of enzyme inhibition and the function of restriction enzymes in DNA cleavage.