Enzymes speed up reactions by binding to reacting molecules, called substrates, to form an enzyme-substrate complex.

The enzyme-substrate complex lines up the substrates in an orientation that stresses or distorts existing chemical bonds, leading to formation of the transition state. In the transition state, the substrates become more reactive and the metabolic reaction accelerates. The site of attachment and the surrounding parts of the enzyme that stress the substrates bonds constitute the enzymes active site. The reaction is complete when the product forms and the enzyme is released in its original condition. The enzyme is then ready to repeat the process with new substrate molecules.

Although enzymes speed up chemical reactions, each enzyme works most efficiently (causes the reaction to occur fastest) under a specific set of conditions. Because almost all enzymes are proteins, any factor that affects the shape of a protein may affect enzyme activity. For example, at high temperatures, proteins denature, or lose their normal shape. Also, the pH of a solution will affect the charge of acidic and basic amino acid side chains on a protein, affecting the interactions that lead to tertiary and quaternary protein structures. In addition to factors that affect protein shape, factors that affect substrate availability can also affect reaction rate. For example, as substrate concentration increases, the reaction rate also tends to increase. This is because the enzymes active site is more likely to be occupied as substrate concentration increases. However, increasing substrate concentration cannot cause the reaction rate to increase indefinitely. Eventually, a point is reached where all available enzymes are saturated and working at maximum efficiency. Therefore, any additional increase in substrate concentration will not produce a corresponding increase in reaction rate. It is at this state of enzyme saturation that the maximum enzyme activity is observed, often referred to as Vmax, for the enzymes maximum velocity.

Factors affecting the rate of enzyme activity Optimum is a useful word which means "the best". We call the temperature or pH which makes an enzyme work at its very fastest the optimum for that enzyme. The rate of enzyme activity increases with as temperature increases until the optimum temperature, then falls to zero as the enzyme is denatured. This means that the protein changes shape and the active site is no longer complementary to the substrate molecule.

pH also affects the rate of enzyme activity. Each enzyme has its own range of pH in which it will work. Two good examples are the enzymes pepsin and catalase. the enzyme pepsin only works between pH 1 - pH 4 (acidic) the enzyme catalase only works between pH 7 - pH 11

At a fixed substrate concentration, an increase in enzyme concentration increases the rate of an enzyme catalyzed reaction until the substrate concentration becomes the limiting factor.

When the substrate concentration is not limiting, the rate of an enzyme catalyzed reaction is directly proportional to the enzyme concentration. The rate slows down when [s] starts becoming limiting factor. The rate remains unchanged at high [E] when [s] is the limiting factor.

Effect of Substrate Concentration

At a fixed enzyme concentration, an increase in f substrate concentration increases the rate of an enzyme catalyzed reaction until the enzyme concentration becomes the limiting factor.

When the enzyme concentration is not limiting, the rate of an enzyme catalyzed reaction is directly proportional to the substrate concentration. on increasing [s] when [E] starts becoming limiting factor, the rate of the enzyme catalyzed reaction slows down. At high [s], the rate remains unchanged because [s] becomes limiting factor.

Effect of pH

Enzymes, being proteins, are affected by the changes in the pH of the reaction medium. Most of the enzymes are, in fact, active only within a narrow range of pH, typically pH 5 to pH 9. The most favorable pH at which an enzyme activity is the maximum is known as the optimum pi I for the enzyme.

The optimum pH value varies from enzyme to enzyme. The pH affects the degree of ionization of the side chains of then amino acid residues of proteins and thereby their three dimensional structure. Furthermore, ionization state of amino acid side chains present in the active site of enzymes are responsible for the catalytic activity of enzymes (see later in this chapter).

The pH also affects the ionization characteristics of the substrates and coenzymes, and thereby, their binding with the enzyme. Thus pH of the reaction medium affects the catalytic activity of the enzyme. The catalytic activity of the enzyme as a function of pH usually appears as a bell-shaped curve.

Effect of Temperature

Like most of the chemical reactions, the rate of an enzyme catalyzed reaction increases with the increase in temperature of the reaction medium.

However, enzymes-being proteins are gradually denatured and lose their activity at the temperature beyond 40 - 50C. Some enzymes, however, remain active even at the temperature as high as 100oC. Each enzyme has an optimum temperature at which its activity is the maximum.

Effect of Inhibitors and Activators

Many molecules and ions, when present in the reaction medium; affect the rate of enzyme-catalyzed reactions. These substances bind to the enzyme or the enzyme-substrate complex, thereby, affecting the rate.

Substances which lower the reaction rate are called enzyme inhibitors and substances which increase the rate are as enzyme activators. Inhibitors and activators are very important in the cellular regulation of enzymes.

Inhibitors can be classified as reversible or irreversible. Reversible inhibitors bind with the enzyme by weak noncovalent bonds and can be removed by dialysis restore the active enzyme. On the other hand irreversible inhibitors bind with enzyme by covalent bonds and cannot be removed from the enzyme by dialysis.

Mechanism of Enzyme Action

Enzymes, as explained before accelerate the rates of biochemical reactions show great deal of substrate specificity. Therefore, any theory on the mechanic enzymatic reaction must take these two facts into account.