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ENZYMES
Most enzymes are huge protein molecules (Tertiary type) that speed biochemical
reactions.
Some enzymes consist of a protein and a helpful nonprotein component called a
prosthetic group. When the prosthetic group is loosely linked to the protein, it is
called a coenzyme. Vitamins are important parts of these coenzymes.
Enzymes are formed at cell sites called ribosomes. Amino acids, the building
blocks of proteins, are brought to the ribosomes and strung together in a precise
manner to form the enzymes. These then float free within the cell or into nearby
body areas where they are needed.
Enzymes can build up or break down other molecules. The molecules they act on
are called substrates. Enzymes are catalysts—chemicals that hasten a chemical
reaction without undergoing any change themselves by lowering the energy of
activation.
Activation Energy: the energy input needed to start chemical reaction.
Enzyme Denature as a result of destruction of tertiary structure, by high
temperature & adverse pH. the protein structure may lose its integrity (denature)
and its enzymatic ability. Denaturation is sometimes, but not always, reversible.

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The lock-and-key model.

The lock-and-key model states that the substrate acts as a 'key' to the 'lock' of the
active site. The active site and substrate are exact matches for each other, similar to
puzzle pieces fitting together. In this model, only a single substrate is the precise
match for the enzyme. Once the enzyme finds its exact counterpart, the chemical
reaction can begin.

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Induced-fit model:

It describes that only the proper substrate is capable of inducing the proper
alignment of the active site that will enable the enzyme to perform its catalytic
function. It also suggests that the active site continues to change until the substrate
is completely bound to it, at which point the final shape and charge is determined.

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Factors affecting enzyme activity:

1-pH:

Enzymes are also sensitive to pH. Changing the pH of its surroundings will also
change the shape of the active site of an enzyme. Each enzyme functions best at
specific pH value.
Most enzymes act maximally at optimum pH around 7 as salivary amylase.
Other enzymes function best at other pH value.

Ex: Pepsin enzyme in stomach has its best activity at pH 2(acidic).

Salivary amylase enzyme in mouth has its best activity at pH 6.8 (neutral).

Alkaline phosphatase enzyme in liver has its best activity at pH 9.5 (alkaline).

2) Temperature:

At 0 C, the number of successful collisions between the enzyme and substrate is

reduced because their molecular movement decreases. The reaction is slow.
Increasing the temperature speeds up the movement of molecules.
Maximum enzyme action at 40 C.
The human body is maintained at 37°C as this is the temperature at which the
enzymes in our body work best. This not true of the enzymes in all organisms.
Enzyme action decreases above 40 C because higher temperatures disrupt the
shape of the active site, which will reduce its activity, or prevent it from
working. The enzyme will have been denatured.
More than 60C, all enzymes are denatured.

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3) Relative of enzyme and substrate:

Substrate concentration

Enzymes will work best if there is plenty of substrate available. As the

concentration of the substrate increases, so does the enzyme activity. This means
that more substrate can be broken down by the enzymes if there is more substrate
available.

This does not mean that the enzyme activity does not increase without end. This is
because the enzyme can't work any faster even though there is plenty of substrate
available. So, when the amount of available substrate exceeds the amount of
enzymes, then no more substrate can be broken down. The enzyme concentration
is the limiting factor slowing the reaction.

Enzyme concentration

As the concentration of the enzyme is increased, the enzyme activity also

increases. This means that more substrate will be broken down if more enzyme is
added.

Again, this increase in enzyme activity does not occur forever. So, when the
amount of available enzyme exceeds the amount of substrate then no more

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substrate can be broken down. The substrate concentration is the limiting factor
slowing the

4) Presence of activators and inhibitors for enzyme:

Activators: are substances that increase enzyme activity, such as co-enzymes

(vitamins) & co-factors (minerals).

Cofactors are non-protein helper molecules attached temporarily or

permanently to the enzyme. For example, the enzyme that builds DNA
molecules, DNA polymerase, requires magnesium ions to function.
Coenzymes are a subset of cofactors that are organic (carbon-based)
molecules. The most common sources of coenzymes are dietary vitamins.
For example, vitamin C is a coenzyme for several enzymes that take part in
building the protein collagen, a key part of connective tissue.

Inhibitors: are molecule that binds to an enzyme and decreases its activity. By
binding to enzymes' active sites, inhibitors reduce the compatibility of substrate
and enzyme and this leads to the inhibition of Enzyme-Substrate complexes'
formation, preventing the catalysis of reactions and decreasing the amount of
product produced by a reaction

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DR. Ali Asar (0109 567 1567)