Enzymes

Enzymes are macromolecular biological catalysts. They are responsible for thousands of metabolic processes that sustain life. Enzymes are highly selective catalysts, greatly accelerating both the rate and specificity of metabolic chemical reactions, from the digestion of food to the synthesis of DNA. Most enzymes are proteins, although some catalytic RNA molecules have been identified. Enzymes adopt a specific three-dimensional structure, and may employ organic (e.g. biotin) and inorganic (e.g. magnesium ion) cofactors to assist in catalysis.

Enzymes act by converting starting molecules (substrates) into different molecules (products). Almost all chemical reactions in a biological cell need enzymes in order to occur at rates sufficient for life. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell, tissue and organ. Organelles are also differentially enriched in sets of enzymes to compartmentalize function within the cell.

Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy (E _a). As a result, products are formed faster and reactions reach their equilibrium state more rapidly. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions and some are so fast that they are diffusion limited. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts in that they are highly specific for their substrates. Enzymes are known to catalyze about 4, 000 biochemical reactions. A few RNA molecules called ribozymes also catalyze reactions, with an important example being some parts of the ribosome. Synthetic molecules called artificial enzymes also display enzyme-like catalysis.

Enzyme activity can be affected by other molecules: decreased by inhibitors or increased by activators. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, pressure, chemical environment (e.g., pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins into smaller molecules, making the meat easier to chew). The study of enzymes is called enzymology.

The term enzyme comes from zymosis, the Greek word for fermentation, a process accomplished by yeast cells and long known to the brewing industry, which occupied the attention of many 19th-century chemists.

Louis Pasteur recognized in 1860 that enzymes were essential to fermentation but assumed that their catalytic action was inextricably linked with the structure and life of the yeast cell. Not until 1897 was it shown by German chemist Edward Bü chner that cell-free extracts of yeast could ferment sugars to alcohol and carbon dioxide; Bü chner denoted his preparation zymase. This important achievement was the first indication that enzymes could function independently of the cell.

The first enzyme molecule to be isolated in pure crystalline form was urease, prepared from the jack bean in 1926 by American biochemist J. B. Sumner, who suggested, contrary to prevailing opinion, that the molecule was a protein. In the period from 1930 to 1936, pepsin, chymotrypsin, and trypsin were successfully crystallized; it was confirmed that the crystals were protein, and the protein nature of enzymes was thereby firmly established.

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