Enzymatic Action

Like all catalysts, enzymes accelerate the rates of reactions while experiencing no permanent chemical modification as a result of their participation. Enzymes can accelerate, often by several orders of magnitude, reactions that under the mild conditions of cellular concentrations, temperature, p H, and pressure would proceed imperceptibly (or not at all) in the absence of the enzyme. The efficiency of an enzyme's activity is often measured by the turnover rate, which measures the number of molecules of compound upon which the enzyme works per molecule of enzyme per second. Carbonic anhydrase, which removes carbon dioxide from the blood by binding it to water, has a turnover rate of 106. That means that one molecule of the enzyme can cause a million molecules of carbon dioxide to react in one second.

Most enzymatic reactions occur within a relatively narrow temperature range (usually from about 30°C to 40°C), a feature that reflects their complexity as biological molecules. Each enzyme has an optimal range of p H for activity; for example, pepsin in the stomach has maximal reactivity under the extremely acid conditions of p H 1–3. Effective catalysis also depends crucially upon maintenance of the molecule's elaborate three-dimensional structure. Loss of structural integrity, which may result from such factors as changes in p H or high temperatures, almost always leads to a loss of enzymatic activity. An enzyme that has been so altered is said to be denatured (see denaturation).

Consonant with their role as biological catalysts, enzymes show considerable selectivity for the molecules upon which they act (called substrates). Most enzymes will react with only a small group of closely related chemical compounds; many demonstrate absolute specificity, having only one substrate molecule which is appropriate for reaction.

Numerous enzymes require for efficient catalytic function the presence of additional atoms of small nonprotein molecules. These include coenzyme molecules, many of which only transiently associate with the enzyme. Nonprotein components tightly bound to the protein are called prosthetic groups. The region on the enzyme molecule in close proximity to where the catalytic event takes place is known as the active site. Prosthetic groups necessary for catalysis are usually located there, and it is the place where the substrate (and coenzymes, if any) bind just before reaction takes place.

The side-chain groups of amino acid residues making up the enzyme molecule at or near the active site participate in the catalytic event. For example, in the enzyme trysin, its complex tertiary structure brings together a histidine residue from one section of the molecule with glycine and serine residues from another. The side chains of the residues in this particular geometry produce the active site that accounts for the enzyme's reactivity.

The Columbia Electronic Encyclopedia, 6th ed. Copyright © 2012, Columbia University Press. All rights reserved.

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