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Specificity of Enzymes

Specificity of Enzymes
One of the most distinctive attributes of enzymes is their high specificity. Specificity is a consequence of the exact molecular fit that is required between enzyme and substrate. Furthermore, an enzyme catalyzes only one reaction. Unlike reactions carried out in an organic chemist’s laboratory, no side reactions or by-products result. Specificity of both substrate and reaction is obviously essential to prevent a cell from being swamped with useless byproducts.

High specificity of trypsin. It splits only peptide bonds adjacent to lysine or arginine.
Figure 4-5 High specificity of trypsin.
It splits only peptide bonds
adjacent to lysine or arginine.
However, there is some variation in degree of specificity. Some enzymes catalyze the oxidation (dehydrogenation) of only one substrate. For example, succinic dehydrogenase catalyzes the oxidation of succinic acid only. Others, such as proteases (for example, pepsin and trypsin), will act on almost any protein, although each protease has its particular point of attack in the protein (Figure 4-5). Usually an enzyme will take on one substrate molecule at a time, catalyze its chemical change, release the product, and then repeat the process with another substrate molecule. The enzyme may repeat this process billions of times until it is finally worn out (after a few hours to several years) and is broken down by scavenger enzymes in the cell. Some enzymes undergo successive catalytic cycles at speeds of up to a million cycles per minute, but most operate at slower rates.