Page 2: Enzyme Action Mechanism

This page details how enzymes interact with their substrates to form complexes. The mechanism involves precise molecular interactions at the active site.

Vocabulary: The enzyme-substrate complex (ES complex) forms when the substrate binds to the enzyme's active site.

Definition: The active site is the specific region of an enzyme where the substrate binds and the reaction occurs.

Highlight: The formation of bonds between the enzyme's amino acids and the substrate is crucial for catalysis.

Page 3: Enzyme Specificity

This page explores the specific nature of enzyme-substrate interactions through the lock-and-key model.

Definition: Enzyme specificity refers to an enzyme's ability to catalyze only specific reactions with particular substrates.

Vocabulary: Catabolism refers to breakdown reactions, while anabolism involves building larger molecules.

Highlight: The three-dimensional shape of the enzyme's active site precisely matches its specific substrate.

Page 4: Induced Fit Model and Cofactors

This page describes the induced fit model and the role of cofactors in enzyme function.

Definition: The induced fit model suggests that the active site molds itself around the substrate during binding.

Vocabulary: Cofactors are non-protein substances required by some enzymes for proper function.

Example: Metal ions like Mg2+ and Fe3+ serve as cofactors by helping to shape the active site.

Page 8: pH Effects and Immobilization

This page covers pH influence on enzymes and introduces immobilization techniques.

Definition: Immobilized enzymes are physically confined within a defined space while maintaining their catalytic activity.

Highlight: Each enzyme has an optimal pH range for maximum activity.