Introduction to Enzymes

The following has been excerpted from a very popular Worthington publication which was originally published in 1972 as the Manual of Clinical Enzyme Measurements. While some of the presentation may seem somewhat dated, the basic concepts are still helpful for researchers who must use enzymes but who have little background in enzymology.

Specificity of Enzymes

One of the properties of enzymes that makes them so important as diagnostic and research tools is the specificity they exhibit relative to the reactions they catalyze. A few enzymes exhibit absolute specificity; that is, they will catalyze only one particular reaction. Other enzymes will be specific for a particular type of chemical bond or functional group. In general, there are four distinct types of specificity:

  • Absolute specificity - the enzyme will catalyze only one reaction.
  • Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino, phosphate and methyl groups.
  • Linkage specificity - the enzyme will act on a particular type of chemical bond regardless of the rest of the molecular structure.
  • Stereochemical specificity - the enzyme will act on a particular steric or optical isomer.

Though enzymes exhibit great degrees of specificity, cofactors may serve many apoenzymes. For example, nicotinamide adenine dinucleotide (NAD) is a coenzyme for a great number of dehydrogenase reactions in which it acts as a hydrogen acceptor. Among them are the alcohol dehydrogenase, malate dehydrogenase and lactate dehydrogenase reactions.

Next: Naming and Classification

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