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Definitions and Concepts for CAIE Biology IGCSE

Topic 5: Enzymes

Definitions in ​bold ​are for supplement only

Active site ​- A specific region of an enzyme where the substrate binds and the
reaction takes place.

Catalyst​ - A substance that increases the rate of a chemical reaction without being changed
itself.

Denaturation​ - Exposure to high temperatures or extremes of pH, produces a permanent


change in the shape of an enzyme’s active site that prevents the binding of a substrate.

Enzyme​ - A biological catalyst that increases the rate of reactions in living organisms.

Enzyme-substrate complex​ - The temporary complex formed when the substrate


binds to the active site of the enzyme.

Rate of reaction ​- The speed at which reactants are converted into products.

Substrate specificity ​-​ ​The ability of an enzyme to catalyse only a specific reaction or set of
reactions which have substrates complementary to the shape of the enzyme.

Substrate specificity ​- The ability of an enzyme to catalyse only a specific reaction or


set of reactions which have substrates complementary to the active site of the
enzyme.

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CIE Biology GCSE

5: Enzymes
Notes

(Content in ​bold​ is for Extended students only)

This work by PMT Education is licensed under https://bit.ly/pmt-cc


https://bit.ly/pmt-edu-cc CC BY-NC-ND 4.0

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https://bit.ly/pmt-edu https://bit.ly/pmt-cc
Enzymes are proteins that act as​ biological catalysts. ​A catalyst is a substance which ​speeds up
the rate of reaction​ in chemical reactions, without being used up. The enzyme is ​not changed
by the reaction and can be used repeatedly. Enzymes are crucial to living organisms as they
speed up m​ etabolic reactions ​which would take​ too long to occur without them​.

Enzyme action:
All enzymes contain an ​active site​, which is a sequence of amino acids with a ​specific shape​.
This shape is ​complementary ​to the substrate. ​When the enzyme breaks the substrate down,
the substrate enters the active site to form an ​enzyme-substrate complex​.​ The substrate is
broken down and the product is released. The enzyme can then bind to another substrate
molecule.

Each enzyme is complementary to only one type of substrate​; hence it cannot break down
other substrates. For example, proteases break down proteins so that amino acids can be
absorbed into the blood. Proteases cannot, however, break down other molecules such as
carbohydrates, which can only be broken down by carbohydrase enzymes.

Factors affecting enzyme action:

● pH​ - enzymes have an o ​ ptimum pH​ that they work best at. As the pH moves away from
this, the ​rate of reaction decreases.​ ​The change in pH causes the​ shape of the active
site to change​. This means that the substrate cannot fit in the active site, hence​ no
enzyme-substrate complexes can form​.​ ​This means that the enzyme has become
denatured​.

● Temperature​ - As the temperature increases up to the enzyme’s optimum, the rate of


reaction increases. ​This is because the molecules have more ​kinetic energy​, thus move
faster. Consequently, ​more successful collisions​ occur, and​ more enzyme-substrate
complexes ​can form.​ ​At very high temperatures above the optimum, the enzymes
become ​denatured ​and the ​active site changes shape​. This decreases the rate of
reaction as ​enzyme-substrate complexes cannot form​.

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