Factors Affecting Enzyme Activity

This page discusses various factors that influence enzyme activity, including temperature, pH, and substrate concentration.

Temperature Effects

Enzymes allow reactions to occur at lower temperatures than they would without the enzyme present. They do this by:

1. Holding substrates close together, reducing repulsion and facilitating bonding.
2. Putting strain on substrate bonds, making them easier to break.

Highlight: Understanding the effect of temperature on enzyme activity is crucial for AQA GCSE Biology enzymes exam questions.

However, excessive heat can lead to enzyme denaturation:

Definition: Denaturing occurs when hydrogen bonds break and the tertiary structure of the enzyme unfolds, rendering the active site non-complementary to the substrate.

pH Effects

The page includes graphs showing the relationship between enzyme activity and pH:

1. A bell-shaped curve illustrating the optimum pH for enzyme activity.
2. A logarithmic scale graph showing enzyme activity across a wider pH range.

Example: The effect of pH on enzyme activity can be demonstrated through practical experiments, often featured in AQA A Level Biology enzymes exam questions.

Enzyme and Substrate Concentration

Graphs illustrate how enzyme and substrate concentrations affect reaction rates:

1. Enzyme concentration: Initially, increasing enzyme concentration increases reaction rate linearly until substrate becomes a limiting factor.
2. Substrate concentration: Reaction rate increases with substrate concentration until enzyme saturation occurs.

Vocabulary: A limiting factor is a variable that constrains the rate of a reaction when other factors are in excess.

Enzyme Inhibitors

This page focuses on enzyme inhibitors, which are substances that reduce enzyme activity.

Types of Inhibitors

There are two main types of reversible inhibitors:

1. Competitive Inhibitors

   • Have a similar shape to the substrate
   • Can occupy the enzyme's active site
   • Compete with the substrate for binding
   • Inhibition depends on relative concentrations of substrate and inhibitor

2. Non-competitive Inhibitors

   • Attach to enzymes away from the active site
   • Alter the shape of the active site
   • Not in direct competition with the substrate
   • Adding more substrate does not decrease their effect

Highlight: Understanding enzyme inhibitors is crucial for AQA A Level Biology students, as it's often featured in exam questions and practical assessments.

Key Points About Enzymes

The page concludes with a summary of essential enzyme characteristics:

• Enzymes are biological catalysts made of globular proteins
• They lower activation energy without being consumed in the reaction
• Enzymes bind to substrates via their complementary active site
• This binding forms an enzyme-substrate complex

Example: The induced fit model vs lock and key comparison is a common topic in A Level Biology courses, illustrating different theories of enzyme-substrate interaction.

Vocabulary: The enzyme-substrate complex is the temporary structure formed when an enzyme binds to its specific substrate during a reaction.