Page 2: Enzyme Inhibition and Activation Energy
The second page delves into different types of enzyme inhibition and explains why enzymes are effective catalysts. It covers both competitive and non-competitive inhibition mechanisms, as well as the role of enzymes in lowering activation energy.
Definition: Non-competitive inhibitors bind to sites other than the active site, causing conformational changes that alter the enzyme's activity.
Example: Common enzyme names often reflect their substrates, such as sucrase for sucrose, maltase for maltose, and lactase for lactose.
Highlight: Enzymes work by weakening chemical bonds, which lowers the activation energy required for reactions to occur.
Vocabulary: Competitive inhibitors are molecules that mimic the substrate and compete for the enzyme's active site, preventing normal substrate binding.



