ENZYMES

 Globular proteins with a 3D shape --> tertiery protein.

 Often larger than a substrate. Only a small part of the enzyme binds to the substrate (the active
site).
 Biological catalysts --> Speed-up reactions by lowering the activation energy.
 Unchanged by reactions. Use them in small amounts.

 Enzymes are denatured by high temperatures.

 They are affected by salt concentration.
 Enzymes are dependant on substrate concentration.

The Lock and Key Theory

The lock and key theory (like the example of enzymes above) describes the enzyme as having a very
specific shape and only a substrate with an exactly complementary shape can fit it. This theory will
explain the specifity of enzymes. Tne enzyme is a lock with will only fit a specific key. Some
enzymes are very specific, eg. Maltase will only fit Maltose. Others (like Lipase) are less specific.

Induced Fit Theory

In this theory, the enzymes active site is thought to be more flexible and changes shape as the
substrate approaches. This can also be explained using the hand and glove analogy.
Factors Effecting Enzyme Activity

pH
the pH can affect the charges of the enzyme. This effects the bonding and the shape of the active site.
the pH can effect the charge of the active site and of the substrate and alters the bonds responsible
for the enzymes tertiery structure.

Only particular substrates will fit becasue they have

opposite/attracting charges and because they are the
right shape.
The presence of an acid (H+) or alkali (OH-) effects enzyme activity. The optimum range of pH tends
to be a narrow band.
Different enzymes have different optimum pH's.
Substrate concentration and the rate of reaction

Competitive and Non-competitive Inhibition

Competitive inhibitors:
 Does not alter the shape of the enzyme
 Inhibition can be reversed by increasing the
concentration of the substrate
 Affects the binding of the of substrate and the
maximum velocity of the enzyme
 Competes with the substrate for the active site of
the enzyme

Non-Competitive inhibitors:
 Inhibition cannot be reversed by increasing
the concentration of the substrate
 Affects only the binding of the substrate
 Alters the shape of the enzyme
 Binds in a different site to the substrate