Temperature

Raising the temperature increases the rate of both uncatalyzed and enzyme-catalyzed reactions by increasing the kinetic energy and the collision frequency of the reacting molecules. However, heat energy can also increase the conformational flexing of the enzyme to a point that exceeds the energy barrier for disrupting the noncovalent interactions that maintain its three-dimensional structure. The polypeptide chain then begins to unfold, ordenature, with an accompanying loss of the catalytic activity. The temperature range over which an enzyme maintains a stable, catalytically competent conformation depends on—and typically moderately exceeds—the normal temperature of the cells in which it resides. Enzymes from humans generally exhibit stability at temperatures up to 45 to 55°C. By contrast, enzymes from the thermophilic microorganisms that reside in volcanic hot springs or undersea hydrothermal vents may be stable at temperatures up to or even above 100°C.

The temperature coefficient (Q10 )is the factor by which the rate of a biologic process increases for a 10°C increase in temperature. For the temperatures over which enzymes are stable, the rates of most biologic processes typically double for a 10°C rise in temperature (Q10 = 2). Changes in the rates of enzyme catalyzed reactions that accompany a rise or fall in body temperature constitute a prominent survival feature for “cold-blooded” life forms such as lizards or fish, whose body temperatures are dictated by the external environment. However, for mammals and other homeothermic organisms, changes in enzyme reaction rates with temperature assume physiologic importance only in circumstances such as fever or hypothermia.

Hydrogen Ion Concentration

The rate of almost all enzyme-catalyzed reactions exhibits a significant dependence on hydrogen ion concentration. Most intracellular enzymes exhibit optimal activity at pH values between 5 and 9. The relationship of activity to hydrogen ion concentration (Figure 1) reflects the balance between enzyme denaturation at high or low pH and effects on the charged state of the enzyme, the substrates, or both. For enzymes whose mechanism involves acid–base catalysis, the residues involved must be in the appropriate state of protonation for the reaction to proceed. The binding and recognition of substrate molecules with dissociable groups also typically involves the formation of salt bridges with the enzyme. The most common charged groups are carboxylate groups (negative) and protonated amines (positive). Gain or loss of critical charged groups adversely affects substrate binding and thus will retard or abolish catalysis.

Fig1. Effect of pH on enzyme activity. Consider, or example, a negatively charged enzyme (E–) that binds a positively charged substrate (SH+). Shown is the proportion (%) of SH+ [\] and of E– [///] as a unction of pH. Only in the cross-hatched area do both the enzyme and the substrate bear an appropriate charge.

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مواضيع ذات صلة

Knowledge of Enzyme Kinetics, Mechanism, and Inhibition Aids Drug Development

The Rates of Reactions are Determined by Their Activation Energy

Ribozymes: Artifacts from the RNA World

The Catalytic Activity of Enzymes Facilitates Their Detection

Chymotrypsin & Fructose-2,6-Bisphosphatase Illustrate Covalent Catalysis

Iron Metabolism

Biochemistry and Biosynthesis of Adrenal Steroids and Testosterone Steroids

Enzymes Employ Multiple Mechanistic Strategies to Facilitate Catalysis

The Oxygen Dissociation Curves for Myoglobin & Hemoglobin Suit Their Physiologic Roles

Heme & Ferrous Iron Confer the Ability to Store & Transport Oxygen

Control of Heme Biosynthesis

Protein Folding