Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. They are neither used up in the reaction nor do they appear as reaction products.
The basic enzymatic reaction can be represented as follows
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where E represents the enzyme catalyzing the reaction, S the substrate, the substance being changed, and P the product of the reaction.
Chemists have known for almost a century that for most chemical reactions to proceed, some form of energy is needed. They have termed this quantity of energy, "the energy of activation." It is the magnitude of the activation energy which determines just how fast the reaction will proceed. It is believed that enzymes lower the activation energy for the reaction they are catalyzing. Figure 3 illustrates this concept.

The enzyme is thought to reduce the "path" of the reaction. This shortened path would require less energy for each molecule of substrate converted to product. Given a total amount of available energy, more molecules of substrate would be converted when the enzyme is present (the shortened "path") than when it is absent. Hence, the reaction is said to go faster in a given period of time.
A theory to explain the catalytic action of enzymes was proposed by the Swedish chemist Savante Arrhenius in 1888. He proposed that the substrate and enzyme formed some intermediate substance which is known as the enzyme substrate complex. The reaction can be represented as:

If this reaction is combined with the original reaction equation [1], the following results:

The existence of an intermediate enzyme-substrate complex has been demonstrated in the laboratory, for example, using catalase and a hydrogen peroxide derivative. At Yale University, Kurt G. Stern observed spectral shifts in catalase as the reaction it catalyzed proceeded. This experimental evidence indicates that the enzyme first unites in some way with the substrate and then returns to its original form after the reaction is concluded.
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