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Enzyme

Regulatory Binding Sites



Regulatory enzymes are characterized by increased or decreased activity in response to chemical signals. Metabolic pathways are regulated by controlling the activity of one or more enzymatic steps along that path. Regulatory control allows cells to meet changing demands for energy and biomolecules. The scheme shown in Figure 5 illustrates the concept of a regulatory feedback mechanism.



Enzymatic activity is regulated in four general ways:

  1. Allosteric control. Allosteric enzymes have distinct binding sites for effector molecules which control their rates of reaction.
  2. Control proteins participate in cellular regulatory processes. For example, calmodulin is a Ca2+ binding protein which binds with high affinity and modulates the activity of many Ca2+-regulated enzymes. In this way, Ca2+ acts as "second messenger" to allow crosstalk and feedback control in metabolic pathways.
  3. Enzyme activity controlled by reversible covalent modification is carried out with a variety of chemical groups. A common example is the transfer of phosphate groups, catalyzed by enzymes known as kinases (Figure 6). Glucose metabolism is modulated by phosphate transfer.
  4. Proteolytic activation. The above example is reversible in nature. Irreversible hydrolytic cleavage of peptide fragments from inactive forms of enzymes known as zymogens converts them into fully active forms. Proteolytic enzymes are controlled by this mechanism.

Resources

Books

Branden, C., and J. Tooze. Introduction to Protein Structure. New York: Garland, 1991.

Lehninger, A.L., D.L. Nelson, and M.M. Cox. Principles of Biochemistry. 2nd ed. New York: Worth, 1993.

Periodicals

Kraut, J. "How Do Enzymes Work?" Science 242 (1988): 533-540.


Leonard D. Holmes

KEY TERMS

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Activation energy

—The amount of energy required to convert the substrate to the transition state.

Active site

—The fold or cleft of an enzyme which binds substrate and catalytically transforms it to product.

Hydrophobic

—Nonpolar, insoluble in water.

Induced fit

—Enzyme conformational change caused by substrate binding and resulting in catalytic activity.

Lock-and-key

—Geometrically complementary shapes of the enzyme (lock) and the substrate (key) resulting in specificity.

Peptide bond

—Chemical covalent bond formed between two amino acids in a polypeptide.

Polypeptide

—A long chain of amino acids linked by peptide bonds.

Rate of reaction

—The quantity of substrate molecules converted to product per unit time.

Transition state

—The activated form of the reactant occupying the highest point on the reaction coordinate.

Weak interactions

—Noncovalent interactions between the substrate and the enzyme, allowing enzyme conformational change and catalysis.

Additional topics

Science EncyclopediaScience & Philosophy: Electrophoresis (cataphoresis) to EphemeralEnzyme - Historical Background Of Enzyme Research, Enzyme Structure, Enzyme Function, Environment, Enzyme Inhibitors, Regulatory Binding Sites - Regulation of enzyme activity