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Enzyme Action Revision Notes

1) An enzyme is a globular protein that acts as a catalyst to speed up chemical reactions without being used up itself. 2) The active site of an enzyme is a complementary shape to the substrate and is responsible for catalytic activity. 3) The lock and key theory and induced fit hypothesis both propose that the substrate fits precisely into the active site to initiate reactions that produce products.

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74 views2 pages

Enzyme Action Revision Notes

1) An enzyme is a globular protein that acts as a catalyst to speed up chemical reactions without being used up itself. 2) The active site of an enzyme is a complementary shape to the substrate and is responsible for catalytic activity. 3) The lock and key theory and induced fit hypothesis both propose that the substrate fits precisely into the active site to initiate reactions that produce products.

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An introduction to enzyme structure and function

An enzyme is a protein. Each and every enzyme is a globular protein with a specific tertiary structure (see 3.4 Amino
Acids and Proteins). They are catalysts – substances which speed up chemical reactions, but do not get used up in the
process.
active site
A single enzyme is quite a large molecule. The whole primary,
secondary and tertiary structures are involved in giving an amino acid in
enzyme its specific shape. That special shape is needed to provide the active site
a certain shape for the active site. This is the area of an enzyme
where the catalytic activity occurs, and is a ‘pocket’ or cleft in the
enzyme’s 3D structure.

Although there are hundreds, if not thousands, of amino acids


found in a single enzyme, very few are responsible for The substrate is a complementary
maintaining the shape of the active site, usually less than ten, as shape to the active site shape
shown in the diagram.

There is only one substrate which is specific enough to fit an enzyme. So each enzyme can catalyse a reaction involving
only one type of substrate. Different enzymes use different substrates. The substrate will be shaped in a way which is
complementary to the shape of the active site. The lock and key theory of enzymes states that the substrate is a “key”
and the enzyme’s active site a “lock” which can only be triggered by that one key that fits.

Lock and Key Theory


substrate

products

enzyme enzyme-substrate complex

This is the generally-accepted model which suggests that only one substrate “the key” will fit one and only one active
site belonging to an enzyme, “the lock”. When the key is inside the lock, the reaction takes place with the substrate
held inside the enzyme, and the result is the products released

Induced-Fit Hypothesis
substrate

products

enzyme enzyme-substrate complex

A more recent explanation to the fitting of enzymes is the induced-fit hypothesis. This hypothesis still states that one
substrate fits one active site, this is scientific fact. But this hypothesis suggests that the enzyme molecule slightly
changes shape when it collides with substrate, making the active site fit more closely around the substrate molecule.
The substrate is held in place, and the reaction takes place in the enzyme-substrate complex. The products made no
longer fit the active site, so they are released, and this enables the enzyme to redo the whole process by taking in
another substrate molecule

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These two theories bring up the idea of product. In a chemical reaction, if an enzyme catalyses the reaction, substrate is
turned into product. The general formula below shows this:
catalyst
substrate product

Take the example of the enzyme maltase. This is able to catalyse the conversion of maltose into glucose:
maltase
maltose glucose + glucose

One maltose molecule is made up of two glucose molecules joined by a single glycosidic bond (see 3.2 Carbohydrates).
If we want to break the component down back into two separate glucose molecules, we need to break that glycosidic
bond up. We can boil maltose in hydrochloric acid to do this. It supplies the maltose molecules with enough energy to
break the bond and collide with water molecules for the hydrolysis reaction to take place. This extra burst of energy
required to initiate a reaction is called activation energy.
Energy

Many biological molecules, like


maltose, are simply too stable to
energy
simply break their bonds out of
provided by
thin air. These large amounts of
boiling in acid
energy are required to do so,
because the bonds are strong,
most of them covalent.
maltose molecule
Boiling in hydrochloric acid
provides the molecule with this
energy, but it is very unlikely
glucose molecules that cells do this naturally and
even if they did, that they would
survive. So how can these
reactions be initiated without
Time the need for such extremes?

A catalyst can be used to drive metabolic reactions. These work by enabling the same reactions more readily, because
they reduce the amount of activation energy required to initiate the reaction. Enzymes are catalysts which reduce the
amount of activation energy needed, so reactions can take place at lower temperatures and in a more diverse range of
conditions. This is the case because the active site of the enzyme molecule can fit the substrate perfectly.

Without catalysts, the metabolic


Energy

activation energy reactions which are essential to


required without enzyme life would not be able to take
activation
place at the right amounts and
energy required at the right speeds, so they are
with enzyme essential substances.

It is important to remember that


maltose molecule
an enzyme is a catalyst, and that
it is part of a chemical reaction,
where it is used to speed up the
reaction – but the enzyme does
glucose molecules
not get used up in the process:
an enzyme can be used many
times, but does eventually
Time become less effective.

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