Chemical Nature of Enzymes

With the exception of a small group of catalytic RNA molecules, all enzymes

are proteins. Like all proteins, enzymes are composed mainly of the 20 naturally

occurring amino acids linked by peptide bonds to form polypeptide chains.

Enzymes show all the properties of protein, i.e., like proteins, enzymes are

chemically made up of amino acids as building-blocks linked by peptide bonds;

can be hydrolyzed to yield a mixture of constituent amino acids; lose catalytic

activity if subjected to extreme pH, temperature, strong acids or bases, organic

solvents or other conditions which denature protein and give typical color tests

like biuret and FCR (Folin-Ciocalteu reagent) reactions. Their catalytic activity

depends on the integrity of their native protein conformation. If an enzyme is

denatured or dissociated into its subunits, catalytic activity is usually lost. If

an enzyme is broken down into its component amino acids, its catalytic

activity is always destroyed. Thus the primary, secondary, tertiary, and

quaternary structures of protein enzymes are essential to their catalytic

activity. Many enzymes consist of more than one polypeptide chain (or subunit)

that aggregate to confer catalytic activity. In some enzymes the subunits are

identical, in others they differ in sequence and structure. This description of

subunit arrangement in such enzymes is called the quaternary structure. A typical

enzyme is not an entity completely folded as a whole, but may consist of

apparently autonomous or semiautonomous folding units called domains

Enzymes, like other proteins, have molecular weights ranging from about

12,000 to more than 1 million.

Some enzymes require no chemical groups for activity other than their amino

acid residues. They are solely proteins while others require an additional

chemical component (Non protein part) called a cofactor. Cofactor may either

be one or more inorganic ions, such as Fe +2, Mg+2, Mn+2, or Zn+2. Such inorganic

and detachable cofactors are termed as Activators. Cofactors may be complex

organic or metalloorganic molecules. If organic cofactors are loosely attached

with protein part they are called a coenzyme, however, covalently attached

organic cofactors are called prosthetic groups. Some enzymes require both a

coenzyme and one or more metal ions for activity.

A complete, catalytically active enzyme together with its bound coenzyme

and/or metal ions is called a holoenzyme. The protein part of such an enzyme

is called the apoenzyme or Apo protein. Coenzymes act as transient carriers

of specific functional groups. Most are derived from vitamins, organic

nutrients required in small amounts in the diet. Finally, some enzyme proteins

are modified covalently by phosphorylation, glycosylation, and other

processes. Many of these alterations are involved in the regulation of enzyme

activity.