1. Enzymes
Over 1000 different reactions can take place in a single cell in any given moment.
Each individual reaction is catalysed by a specific enzyme.
Enzymes are very specific.

2. A reaction occurs when chemical bonds of inputs or reactants are broken and the atoms recombine to form a new substance or substances.

3. Biochemical Pathways
All metabolic reactions that occur in cells are controlled and regulated to maintain cell functions and to meet the energy needs of a cell. Done through biochemical pathways.
Each step controlled by an enzyme.

4. A+B (reactants) = C+D (products)
For A+B to equal C+D a certain amount of energy is required before this reaction can occur. Called activation energy.
For cells to continue functioning enough energy must be provided to maintain the process of generating products from reactants & must control rate of energy released so they do not burn up.

5. Biochemical reactions go through a series of steps where the product of one step becomes the reactant for the next step  the product from one reaction is continually removed by being the reactant for the next reaction.

6. Enzymes Cells use enzymes to speed up reactions
Enzymes interact with substrate molecules (reactants) to increase rate of reaction.
Enzymes are not consumed in a reaction and therefore can be recycled.
Without enzymes the reactions that occur in living organisms would be so slow and hardly work at all.

7. Naming Enzymes
Intracellular enzymes: speed up and control metabolic reactions inside the cell.
Extracellular enzymes: secreted from cell and catalyse reactions outside the cell.
Named by attaching ‘– ase’ to the substrate on which it acts.
Carbohydrases act on carbohydrates
Lipases act on Lipids
Proteases acts on Protein
Nucleases act on nucleic acids
ATPase acts on ATP

8. Enzyme Power Work fast Catalase is one of the fastest
Found in liver where it speeds up the breakdown of hydrogen peroxide (H2O2) into oxygen and water.
2 H2O2  2H2O + O2 (balanced equation)

9. Catalase reduces the activation energy needed to break down hydrogen peroxide. Enzymes are powerful because they reduce the activation energy for chemical reactions.

10. Enzymes
The folding of an enzyme protein into its tertiary structure forms an actual groove or pocket.
This grove can accommodate one or more substrate molecules called an active site.
Active site = highly specific for a particular substrate & needs to be a compatible shape for binding to occur.
Lock & Key Model

11. Cofactors and Coenzymes
Cofactors: small inorganic substances (e.g. zinc ions and magnesium ions) that need to be present in addition to an enzyme to catalyse a certain reaction
Coenzymes: non-protein organic substances that are required for enzyme activity.
Small molecules compared to the enzyme
Major role in metabolic pathways
Can function as a carrier, donor or acceptor of a substance involved in the reaction and/or may bind with an enzyme to activate it.

12. Factors affecting enzyme activity
Enzymes are sensitive to changes in substrate and product concentrations, temperature, pH and other substances that may compete with a substrate for an active site.

13. Temperature Work best in temperatures that they are found.
Human body = 37 ˚C
Enzymes require less energy to work due to their flexible structure.

14. How does temperature change affect enzyme activity?
Increase in temp = increase in activity
Increase in activity = increase in collisions between substrate and enzyme  faster rate of reaction.
If temperature is too high, bonds break and the protein loses it’s functional shape.
The enzyme can no longer bind with the active site of the substrate.
Enzymes are not denatured at low temperatures.

15. Effect of pH Each enzyme has an optimum pH at which it works.
Most work effectively at pH7 (neutral)
Optimal pH of an enzyme relates to the environment in which it works. E.g. pepsin in the stomach (pH1.5).
Catalase works in a neutral environment of cells in the liver (pH 7).
Alkaline Phosphatase in bone (pH 9.5).

16. Effect of substrate and enzyme concentration
Amount of substrate or enzyme present in a reaction mix can limit the amount of product produced.
Increased substrate  more products made until all enzyme molecules are working at their maximum capacity.

17. Inhibiting the work of enzymes
Some enzymes have 2 or more active sites for enzymes
Activity of almost every enzyme in a cell is regulated by feedback inhibition where the product of the reaction can inhibit enzyme activity.
Inhibitor binds to enzyme  active site changing shape, therefore cannot bind to substrate.

18. Inhibitors
Non-competitive inhibitor: a molecule that binds to an enzyme at a site other than the active site which changes the shape of the enzyme so that the substrate can no longer bind to the active site.
Competitive inhibitor: a substance that competes with a substrate for an enzyme’s active site.
Examples: poisons whereby the inhibitor binds to the active site preventing the enzyme from catalysing reactions and overtime this concentration of enzyme reduces and the reactions stop.