Enzyme Characteristics and Binding Sites

Enzyme Characteristics

• Enzymes function as catalysts, speeding up chemical reactions without altering themselves.
• All enzymes are proteins, constructed from sequences of amino acids.
• Each enzyme is specific to a substrate, exemplified by the "lock and key" model.
• Enzymes often work alongside coenzymes, non-protein molecules (e.g., vitamins) that enhance enzyme activity.
• They are reusable and can participate in multiple chemical reactions.
• Enzymes lower the activation energy required for reactions, facilitating faster progress.

Binding Sites

• Enzymes have two critical binding sites:
  • Active site: where the substrate binds, allowing the reaction to occur.
  • Allosteric site: where inhibitors (toxins) attach, reducing or halting enzyme activity.

Substrates and Denaturation

• A substrate is the specific substance upon which an enzyme acts.
• Denaturation refers to the alteration of enzyme structure, particularly due to high temperatures (above 50°C), affecting the active site.

Enzyme-Substrate Interaction

• The interaction is explained by the Induced Fit Model, where the active site undergoes a conformational change to fit the substrate precisely.

Enzyme Activity Factors

• pH Levels: Each enzyme has an optimum pH where it performs best.
• Temperature: Each enzyme operates optimally at a specific temperature (typically around 37°C for human enzymes).
• Enzyme Concentration: Increasing enzyme concentration can enhance reaction rates, provided there's sufficient substrate.
• Inhibitors: Molecules that decrease enzyme activity, impacting overall reaction rates.

Nucleic Acids

• Nucleic acids contain carbon (C), hydrogen (H), oxygen (O), nitrogen (N), and phosphorus (P).
• They are polymers made of nucleotides, which consist of three components:
  • A phosphate group
  • A five-carbon sugar
  • A nitrogen base

Enzyme Characteristics

• Enzymes function as catalysts, speeding up chemical reactions without altering themselves.
• All enzymes are proteins, constructed from sequences of amino acids.
• Each enzyme is specific to a substrate, exemplified by the "lock and key" model.
• Enzymes often work alongside coenzymes, non-protein molecules (e.g., vitamins) that enhance enzyme activity.
• They are reusable and can participate in multiple chemical reactions.
• Enzymes lower the activation energy required for reactions, facilitating faster progress.

Binding Sites

• Enzymes have two critical binding sites:
  • Active site: where the substrate binds, allowing the reaction to occur.
  • Allosteric site: where inhibitors (toxins) attach, reducing or halting enzyme activity.

Substrates and Denaturation

• A substrate is the specific substance upon which an enzyme acts.
• Denaturation refers to the alteration of enzyme structure, particularly due to high temperatures (above 50°C), affecting the active site.

Enzyme-Substrate Interaction

• The interaction is explained by the Induced Fit Model, where the active site undergoes a conformational change to fit the substrate precisely.

Enzyme Activity Factors

• pH Levels: Each enzyme has an optimum pH where it performs best.
• Temperature: Each enzyme operates optimally at a specific temperature (typically around 37°C for human enzymes).
• Enzyme Concentration: Increasing enzyme concentration can enhance reaction rates, provided there's sufficient substrate.
• Inhibitors: Molecules that decrease enzyme activity, impacting overall reaction rates.

Nucleic Acids

• Nucleic acids contain carbon (C), hydrogen (H), oxygen (O), nitrogen (N), and phosphorus (P).
• They are polymers made of nucleotides, which consist of three components:
  • A phosphate group
  • A five-carbon sugar
  • A nitrogen base