g9 Igcse Biology
g9 Igcse Biology
g9 Igcse Biology
f. The shape of the active site is ‘complementary’ to its substrates – this means that the
substrate(s) fits into the enzyme in the same way a key fits into a lock. This
complementary nature is what makes the enzyme specific to a substrate.
g. So, in a reaction, the substrate will be randomly moving around. As a result of this
random motion, the substrate will collide with and bind to an enzyme that it is specific to.
This results in the formation of an enzyme-substrate complex. The enzyme then catalyses
the reaction – either breaking up a substrate (a catabolic reaction) or joining two
substrates together (an anabolic reaction).
h. It then releases the products, to make space for more substrates, so that the enzyme can
catalyse more reactions.
5. Investigate and describe the effect of changes in temperature and pH on enzyme activity with
reference to optimum temperature and denaturation
a. Raising temperature generally speeds up a reaction, and lowering temperature slows
down a reaction. However, extreme high temperatures can cause an enzyme to lose its
shape (denature) and stop working. pH: Each enzyme has an optimum pH range.
Changing the pH outside of this range will slow enzyme activity.
6. Explain enzyme action with reference to: active site, enzyme-substrate complex, substrate and
product
a. The induced fit model states an substrate binds to an active site and both change shape
slightly, creating an ideal fit for catalysis. When an enzyme binds its substrate it forms an
enzyme-substrate complex
7. Explain the specificity of enzymes in terms of the complementary shape and fit of the active site
with the substrate
a. The positions, sequences, structures, and properties of these residues create a very
specific chemical environment within the active site. A specific chemical substrate
matches this site like a jigsaw puzzle piece and makes the enzyme specific to its
substrate.
8. Explain the effect of changes in temperature on enzyme activity in terms of kinetic energy, shape
and fit, frequency of effective collisions and denaturation
a. Above a certain temperature (above the optimum point ~37 degrees) the high temp breaks
the Hydrogen bonds in the active sight, changing the shape of the enzyme, so it can no
longer bind to its substrate . The reaction slows and stops. The enzyme no longer works,
this is known as DENATURING.
9. Explain the effect of changes in pH on enzyme activity in terms of shape and fit and denaturation
a. Enzymes function best at their optimum pH. The further away the pH of the environment
is from the enzyme's optimum pH, the more enzymes slow down and denature. This
causes the active site to lose its shape, so the substrate(s) can no longer fit into the active
site. This causes enzyme activity to fall.