Biology 4.

5 ENZYMES

Enzymes are proteins which act as biological catalysts. They speed up biochemical reactions in the cell. The substance whose reactivity is increased by an enzyme is known as substrate. Example:

substrate enzyme> products

sucrose + water sucrase> glucose + fructose

Thousands of simultaneous biochemical reactions occur in living cells. Without enzymes, these biochemical reactions would be too slow to sustain life.

General characteristics of enzymes

1. Enzymes work very rapidly

One molecule of enzyme can turn thousands or millions of substrate molecules into products per minute. For example, catalyse can transform approximately six million hydrogen peroxide molecules into oxygen and water molecules per minute. 2. Enzymes are not destroyed by the reactions which that catalyse

Since enzymes are not altered by the reactions they catalysed, they can be used again. A smaill concentration of enzymes can bring about a large amount of biochemical reactions 3. Enzyme-catalysed reactions are reversible

lactose + water lactase> glucose + galactose lactose + water <lactase glucose + galactose The enzyme which catalyses a reaction works in such a way that the reaction can proceed from left to right or from right to left, depending on circumstances. Note the two way arrows.

4. Enzymes are extremely specific

Most enzymes are specific to one particular substrate molecule. Thus, a given enzyme will catalyse only one reaction or one type of reaction. Maltase, for example, acts only on maltose. 5. Enzymes are denatured by high temperature

An enzyme inactive at very low temperature. As temperature rises, its activity increases until the optimum temperature is reached. The optimum temperature is around 40 C. Above the optimum temperature, the rate of reaction decline rapidly, ceasing altogether at about 60 C. This is because enzymes are made of protein, so they are denatured at high temperature. When an enzyme becomes denatured, the bonds are broken and the polypeptide chains open up. The enzyme loses its normal shape and becomes inactive. 6. Enzymes are sensitive to pH

Every enzymes has its own optimum pH in which it functions best. Small changes in the pH of the medium will denature the enzyme and render its activity. Alterations in the ionic charges of the acidic and basic groups of the enzyme change the shape of the enzyme.

Naming of enzymes based on the substrate

An enzyme is named by attaching the suffix -ase to the name of the substrate on which it acts. For example, maltase acts on maltose, sucrase on sucrose and cellulase on cellulose. The -ase rule does not apply to enzymes discovered before the -ase idea was introduced. For example, pepsin rennin, ptyalin and trypsin.

Intracellular and extracellular enzymes

Enzymes can be divided into two groups: intracellular and extracellular. Enzymes formed and retained in the cell are known as intracellular enzymes, and occur in the cytoplasm, organelles or the nucleus. Examples of intracellular enzyme are DNA polymerase, RNA polymerase and ATP synthetase. Extracellular enzymes are produced in the cell then packed and secreted from the cell, Extracellular enzymes caralyse their reactions outside the cell. Most digestive enzymes are extracellular enzymes. For example, amylase, cellulase and zymase.

Site of Enzyme Synthesis

Since enzymes are made of proteins, they are synthesised by ribosomes. Intracellular enzymes are synthesised on free ribosomes. Extracellular enzymes are synthesised on ribosomes attached to the endoplasmic reticulum.

Formation and secretion of extracellular enzymes: 1. The instruction for making the extracellular enzyme is transcribes from deoxyribonucleic acid (DNA) to ribonucleic acid (RNA) in the nucleus. 2. The RNA then leaves the nucleus through the nuclear pore and attaches itself to the ribosome located on the endoplasmic reticulum. 3. When the enzyme synthesis has completed, it is extruded into the interior of the endoplasmic reticulum. 4. The enzyme is then encapsulated in a transport vesicle. 5. The transport vesicle fuses with the Golgi apparatus, releasing the enzyme into the Golgi apparatus. 6. In the Golgi apparatus the enzyme is further modified before packing the enzyme in a secretory vesicle. 7. The secretory vesicle transports the enzyme to the plasma membrane. 8. The secretory vesicle membrane fuses with the plasma membrane and the enzyme is release outside the cell.

Mechanism of enzyme action

Each enzyme molecule has a region with very precise shape called the active site. The substrate molecule fits into the active site of the enzyme like a key into a lock. Various types of bonds including hydrogen bonds and ionic bonds hold the substrate(s) in the active site to form a enzymesubstrate complex. The enzyme then changes the substrate(s) either by splitting it apart (for example, hydrolysis) or linking them together (for example, condensation) Once formed, the products no longer fit into the active site and escape into the surrounding medium, leaving the active site free to receive further substrate molecules.

enzyme+substrate enzyme-substrate complex> enzyme+product

The explanation of enzyme action is known as the lock and key hypothesis, where the substrate is like a key whose shape is complementary to the enzyme or lock. The lock and key hypothesis is able to explain why enzymes are specific and why any change in enzyme shape alters its effectiveness.

Factors afftecting enzymes 1. pH

Most enzymes are effective in only a narrow pH range. The optimum pH is the particular pH at which the rate of reaction is the highest. Deviations from the optimum pH decrease the rate of reaction because bonds maintaining the tertiary shape of the enzyme are broken. The active site loses its shape and the enzyme-substrate complex can no longer be formed. The enzyme is denatured.

2. Temperature

Initially an increase in temperature leads to an increase in the rate of reaction because the kinetic energy of the enzyme and substrate molecules produce more collisions, and therefore more enzyme-substrate complexes are formed. The rate of reaction will increase up to a maximum, known as the optimum temperature. After the optimum temperature, the rate of reaction falls quickly because the bonds maintaining the structure of the enzyme start to break and the active site loses its shape. The enzyme-substrate complexes can no longer form and the enzyme is denatured.

Substrate Concentration

Initially an increase in substrate concentration increases the chance of enzyme-substrate collisions, and the rate of reaction increases. Eventually all the active sites are filled at any one time and the rate remains constant The reaction has reached its maximum rate, Vmax. Further addition of substrate will not increase the rate of reaction anymore because the constant enzyme concentration becomes the limiting factor.

4. Enzyme Concentration

As the concentration of the enzyme increases there are more chances of enzyme-substrate collisions. The rate of reaction increases linearly as long as no other factors are limiting. As more active sites are available, more substrates can be converted to products.