BY1.

4 Enzymes
Information
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in class?
Revised
for EUT?
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1
The general characteristics of enzymes are due to their biochemical nature as globular proteins, showing specificity,
requiring certain conditions and with a mode of action lowering the activation energy of a reaction

2
The substrate binds to part of the protein called the active site. The shape of the substrate is complementary to
the shape of the active site

3
Candidates should understand the action of enzymes explained in relation to enzyme structure - lock and key
hypothesis; the theory of induced fit whereby the specific substrate for the enzyme alters the shape of the active
site on binding as illustrated by lysozyme (structural details not required)

4
Enzymes are proteins made inside living cells but may act either inside the cell (intracellular) or outside the cell
(extracellular) such as the digestive enzymes of the alimentary canal

5
The rate of an enzyme catalysed reaction increases with increasing temperature due to increased kinetic energy
causing higher frequency of successful collisions between active sites and substrate molecules (as shown by a
graph)*
6
Enzymes have an optimum temperature at which they work best. This is a balance between having high kinetic
energy (causing many successful collisions between active site and substrate) but NOT affecting the tertiary shape of
the enzyme
7
High temperatures cause permanent change in protein structure, causing denaturation. The enzyme molecules
vibrate at higher temperatures above the optimum, breaking the Hydrogen bonds between some R groups. This
permanently changes the shape of the enzyme's active site.

8
The rate of an enzyme catalysed reaction will vary with changes in pH (as shown by a graph)*. Each enzyme will
have an optimum pH at which it works best.

9
Small changes in pH away from the optimum cause small reversible changes in enzyme structure, causing
inactivation
10
The small pH changes cause a change in electrostatic charges on the R groups in the active site of the enzyme,
making it inactive (these enzymes can become active again if the pH is changed back to the optimum)

11
Large or extreme changes in pH away from the optimum will break the ionic bonds within the tertiary structure of
the enzyme, altering its shape and permanently denaturing the enzyme

12 The rate of an enzyme catalysed reaction will vary with changes in enzyme concentration (as shown by a graph)*

13 The rate of an enzyme catalysed reaction will vary with changes in substrate concentration (as shown by a graph)*

14
Candidates should be aware of the need for buffers in enzyme experiments and the requirement for adequate
controls. A buffer is a chemical that will ensure the pH of a solution stays the same

15
Environmental conditions such as temperature and pH change the three dimensional structure of enzyme
molecules. Bonds are broken and hence the configuration (shape) of the active site is altered (SEE 7 AND 11 ABOVE)

16 Inhibition is when enzyme action is slowed down or stopped by another substance

17
Enzyme inhibition may be competitive whereby an inhibitor, which is structurally similar to the substrate,
temporarily binds with the enzyme active site. This blocks the substrate from binding. If the substrate concentration
is increased so will the rate of reaction (as shown by a graph)*

18
Non-competitive inhibition involves an inhibitor combining away from the active site often altering the enzyme
shape as illustrated by potassium cyanide. The rate of reaction is unaffected by substrate concentration (as shown
by a graph)*




*You must study the different enzyme graphs and be able to describe what is happening in
each case