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CONTROL IN CELLS

Enzymes
Enzymes can be defined as biological catalysts. A catalyst is a substance which speeds up a chemical reaction
but remains unchanged itself at the end. Enzymes are biological catalysts because they are protein molecules
made by living cells. A typical human cell contains several thousand enzymes. They are used to catalyse a vast
number of chemical reactions at temperatures unsuitable for living organisms, that is between approximately 5
and 40 oC. High temperatures would be needed, as well as marked changes in other conditions, if the same
speeds of reaction were to be achieved outside the organisms. These would be lethal to a living cell. Enzymes
are vitally important because in their absence reactions in the cell would be too slow to sustain life.
The chemical (or chemicals) which an enzyme works on is called its substrate. An enzyme combines
with its substrate to form a short-lived enzyme/substrate complex. This proximity of the enzyme with the
substrate in the complex greatly increases the chances of a reaction occurring. Once a reaction has occurred, the
complex breaks up into products ad enzyme. The enzyme remains unchanged at the end of the reaction and is
free to interact again with more substrate.
Substrate +enzyme enzyme/substrate complex enzyme/product complex enzyme/product (s)
Properties of enzymes
Enzymes possess the following major properties:

All are globular proteins.


Being proteins, they are coded for by DNA.

Their presence does not alter the nature or properties of the end product (s) of the reaction.

They are very efficient. In other words, a very small amount of catalyst brings about the change of a large amount of
substrate. For example, one molecule of the enzyme catalase can catalyse the decomposition of about 600 thousand
molecules per second of hydrogen peroxide to water and oxygen at body temperature.
They are highly specific, that is an enzyme will generally catalyse only a single reaction. Catalase, for example, will only
catalyse the decomposition of hydrogen peroxide.
The catalysed reaction is reversible. Their activity is affected by pH, temperature, substrate concentration and enzyme
concentration.
Enzymes lower the activation energy of the reactions they catalyse.
Enzymes possess active sites where the reaction takes place. These sites have specific shapes.

The activation energy barrier


The amount of energy required by the substrate molecules before they can undergo the chemical reaction.

The initial investment of energy for starting a reaction, that is, the energy required to break bonds in the reactant molecules is
known as the free energy of activation, or activation energy. It is usually provided in the form of heat that the reactant
molecules absorb from the surroundings. The bonds of the reactants break only when the molecules have absorbed enough
energy to become unstable.
Enzymes and activation energy
Enzymes, by functioning as catalysts, serve to lower/reduce the activation energy required for a chemical reaction to take
place. They speed up the overall rate without altering, to any great extent, the temperature at which it occurs.

Mechanism of enzyme action


The lock and key mechanism (suggested by Fischer in 1890)
Most enzymes are far larger molecules than the substrates they act on.
Within the surface structure of each enzyme is an area known as the active site. It may involve only a small number of amino
acids (between 3 and 12 amino acids/catalytic amino acids). The remaining amino acids, which the make up the bulk of the
enzyme, function to maintain the correct globular shape of the molecule.
The active site has a very specific shape, which gives each enzyme its specificity, as only one substrate or type of substrate
with the right shape (whose shape is complementary to the enzyme) will fit exactly into the active site.
The enzyme and substrate fit together to form the enzyme-substrate complex, as a key fits into a lock. In this complex the
substrate is enabled to react at a lower activation energy. This may be due to bonds within it being distorted and stressed in
the complex, so making them more likely to react.

Once the reaction has been catalysed, the products are no longer the right shape to fit properly in the active site and the
complex breaks up, releasing the products and freeing the enzyme for further catalytic action.