What did he discover?
The first enzyme to be isolated was discovered in 1926 by American chemist James Sumner, who crystallized the protein. The enzyme was urease, which catalyzes the hydrolytic decomposition of urea, a component of urine, into ammonia and carbon dioxide.
His discovery was ridiculed at first because nobody believed that enzymes would behave the same way that other chemicals did. Sumner was eventually proven right and won the Nobel Prize in Chemistry in 1946.
An enzyme is a protein that acts as a biological catalyst. Recall that a catalyst is a substance that increases the rate of a chemical reaction without itself being consumed in the reaction. Cellular processes consist of many chemical reactions that must occur quickly in order for the cell to function properly. Enzymes catalyze most of the chemical reactions that occur in a cell. A substrate is the molecule or molecules on which the enzyme acts. In the urease catalyzed reaction above, urea is the substrate. The Figure below diagrams a typical enzymatic reaction.
The first step in the reaction is that the substrate binds to a specific part of the enzyme molecule. The binding of the substrate is dictated by the shape of each molecule. Side chains on the enzyme interact with the substrate in a specific way, resulting in the making and breaking of bonds. The active site is the place on an enzyme where the substrate binds. An enzyme folds in such a way that it typically has one active site, usually a pocket or crevice formed by the folding pattern of the protein. Because the active site of an enzyme has such a unique shape, only one particular substrate is capable of binding to that enzyme. In other words, each enzyme catalyzes only one chemical reaction with only one substrate. Once the enzyme/substrate complex is formed, the reaction occurs and the substrate is transformed into products. Finally, the product molecule or molecules are released from the active site. Note that the enzyme is left unaffected by the reaction and is now capable of catalyzing the reaction of another substrate molecule.
An inhibitor is a molecule which interferes with the function of an enzyme, either by slowing or stopping the chemical reaction. Inhibitors can work in a variety of ways, but one of the most common is illustrated in the Figure below.
The inhibitor binds competitively at the active site and blocks the substrate from binding. Since no reaction occurs with the inhibitor, the enzyme is prevented from catalyzing the reaction. Cyanide is a potent poison which acts as a competitive inhibitor. It binds to the active site of the enzyme cytochrome c oxidase and interrupts cellular respiration. The binding of the cyanide to the enzyme is irreversible and the affected organism dies quickly.
A non-competitive inhibitor does not bind at the active site. It attaches at some other site on the enzyme and changes the shape of the protein. This shift in three-dimensional structure alters the shape of the active site so that the substrate will no longer fit in the site properly (see Figure below).
Some enzymes require the presence of a non-protein molecule called a cofactor in order to function properly. Cofactors can be inorganic metal ions or small organic molecules. Many vitamins, such as B vitamins, act as cofactors. Some metal ions which function as cofactors for various enzymes include zinc, magnesium, potassium, and iron.
- Enzyme is defined.
- An overview of the enzyme reaction process is illustrated.
- Competitive and non-competitive inhibitors are described.
- The role of a cofactor is described.
Watch the animation at the site below and take the quiz:
- What is the substrate?
- How does a competitive inhibitor work?
- How does a non-competitive inhibitor work?