Enzymes - How it works

Amino Acids, Proteins, and Biochemistry

Amino acids are organic compounds made of carbon, hydrogen, oxygen, nitrogen, and (in some cases) sulfur bonded in characteristic formations. Strings of 50 or more amino acids are known as proteins, large molecules that serve the functions of promoting normal growth, repairing damaged tissue, contributing to the body's immune system, and making enzymes. The latter are a type of protein that functions as a catalyst, a substance that speeds up a chemical reaction without participating in it. Catalysts, of which enzymes in the bodies of plants and animals are a good example, thus are not consumed in the reaction.

Catalysts

In a chemical reaction, substances known as reactants interact with one another to create new substances, called products. Energy is an important component in the chemical reaction, because a certain threshold, termed the activation energy, must be crossed before a reaction can occur. To increase the rate at which a reaction takes place and to hasten the crossing of the activation energy threshold, it is necessary to do one of three things.

The first two options are to increase either the concentration of reactants or the temperature at which the reaction takes place. It is not always feasible or desirable, however, to do either of these things. Many of the processes that take place in the human body, for instance, normally would require high temperatures—temperatures, in fact, that are too high to sustain human life. Imagine what would happen if the only way we had of digesting starch was to heat it to the boiling point inside our stomachs! Fortunately, there is a third option: the introduction of a catalyst, a substance that speeds up a reaction without participating in it either as a reactant or as a product. Catalysts thus are not consumed in the reaction. Enzymes, which facilitate the necessary reactions in our bodies without raising temperatures or increasing the concentrations of substances, are a prime example of a chemical catalyst.

THE DISCOVERY OF CATALYSIS.

Long before chemists recognized the existence of catalysts, ordinary people had been using the chemical process known as catalysis for numerous purposes: making soap, fermenting wine to create vinegar, or leavening bread, for instance. Early in the nineteenth century, chemists began to take note of this phenomenon. In 1812 the Russian chemist Gottlieb Kirchhoff (1764-1833) was studying the conversion of starches to sugar in the presence of strong acids when he noticed something interesting.

When a suspension of starch (that is, particles of starch suspended in water) was boiled, Kirchhoff observed, no change occurred in the starch. When he added a few drops of concentrated acid before boiling the suspension, however, he obtained a very different result. This time, the starch broke down to form glucose, a simple sugar (see Carbohydrates), whereas the acid—which clearly had facilitated the reaction—underwent no change. In 1835 the Swedish chemist Jöns Berzelius (1779-1848) provided a name to the process Kirchhoff had observed: catalysis, derived from the Greek words kata ("down") and lyein ("loosen"). Just two years earlier, in 1833, the French physiologist Anselme Payen (1795-1871) had isolated a material from malt that accelerated the conversion of starch to sugar, for instance, in the brewing of beer.

The renowned French chemist Louis Pasteur (1822-1895), who was right about so many things, called these catalysts ferments and pronounced them separate organisms. In 1897, however, the German biochemist Eduard Buchner (1860-1917) isolated the catalysts that bring about the fermentation of alcohol and determined that they were chemical substances, not organisms. By that time, the German physiologist Willy Kahne had suggested the name enzyme for these catalysts in living systems.

Substrates and Active Sites

Each type of enzyme is geared to interact chemically with only one particular substance or type of substance, termed a substrate. The two parts fit together, according to a widely accepted theory introduced in the 1890s by the German chemist Emil Fischer (1852-1919), as a key fits into a lock. Each type of enzyme has a specific three-dimensional shape that enables it to fit with the substrate, which has a complementary shape.

The link between enzymes and substrates is so strong that enzymes often are named after the substrate involved, simply by adding ase to the name of the substrate. For example, lactase is the enzyme that catalyzes the digestion of lactose, or milk sugar, and urease catalyzes the chemical breakdown of urea, a substance in urine. Enzymes bind their reactants or substrates at special folds and clefts, named active sites, in the structure of the substrate. Because numerous interactions are required in their work of catalysis, enzymes must have many active sites, and therefore they are very large, having atomic mass figures as high as one million amu. (An atomic mass unit, or amu, is approximately equal to the mass of a proton, a positively charged particle in the nucleus of an atom.)

Suppose a substrate molecule, such as a starch, needs to be broken apart for the purposes of digestion in a living body. The energy needed to break apart the substrate is quite large, larger than is available in the body. An enzyme with the correct molecular shape arrives on the scene and attaches itself to the substrate molecule, forming a chemical bond within it. The formation of these bonds causes the breaking apart of other bonds within the substrate molecule, after which the enzyme, its work finished, moves on to another uncatalyzed substrate molecule.

Coenzymes

All enzymes belong to the protein family, but many of them are unable to participate in a catalytic reaction until they link with a non protein component called a coenzyme. This can be a medium-size molecule called a prosthetic group, or it can be a metal ion (an atom with a net electric charge), in which case it is known as a cofactor. Quite often, though, coenzymes are composed wholly or partly of vitamins. Although some enzymes are attached very tightly to their coenzymes, others can be parted easily; in either case, the parting almost always deactivates both partners.

The first coenzyme was discovered by the English biochemist Sir Arthur Harden (1865-1940) around the turn of the nineteenth century. Inspired by Buchner, who in 1897 had detected an active enzyme in yeast juice that he had named zymase, Harden used an extract of yeast in most of his studies. He soon discovered that even after boiling, which presumably destroyed the enzymes in yeast, such deactivated yeast could be reactivated. This finding led Harden to the realization that a yeast enzyme apparently

consists of two parts: a large, molecular portion that could not survive boiling and was almost certainly a protein and a smaller portion that had survived and was probably not a protein. Harden, who later shared the 1929 Nobel Prize in chemistry for this research, termed the non protein a coferment, but others began calling it a coenzyme.