MBC 301: ENZYMOLOGY AND
CLINICAL BIOCHEMISTRY
Introduction to enzymes. Classification
of enzymes, Cofactors, coenzymes,
prosthetic groups, Properties of
enzymes, Factors affecting enzyme
activity
Introduction to enzymes
• Enzymes are organic catalysts which are either protein or protein
containing compounds they are biological catalysts or biocatalyst.
• They are compounds that increase the rate of chemical reactions.
• Enzyme catalysts bind reactants (substrates), convert them to products,
and release the products.
• Although enzymes may be modified during their participation in this
reaction sequence, they return to their original form at the end.
• In addition to increasing the speed of reactions, enzymes provide a
means for regulating the rate of metabolic pathways in the body.
• A catalyst is a substance which alter the rate of a chemical reaction which
itself does not undergo a permanent chemical change.
• With the exception of a few classes of catalytic RNA molecules, all
enzymes are proteins.
• 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.
• 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. Others require an additional chemical component called a cofactor—
either one or more inorganic ions, such as Fe2+, Mg2+, Mn2+, or Zn2+ , or a
complex organic or metalloorganic molecule called a coenzyme.
• Coenzymes act as transient carriers of specific functional groups. Most are derived
from vitamins, organic nutrients required in small amounts in the diet.
• Some enzymes require both a coenzyme and one or more metal ions for activity.
• A coenzyme or metal ion that is very tightly or even covalently bound to the
enzyme protein is called a prosthetic group.
• 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 apoprotein.
• 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.
Classification of enzymes
• Many enzymes have been named by adding the suffix “-ase” to the name of their
substrate or to a word or phrase describing their activity. Thus urease catalyzes
hydrolysis of urea, and DNA polymerase catalyzes the polymerization of
nucleotides to form DNA.
• Other enzymes were named by their discoverers for a broad function, before the
specific reaction catalyzed was known.
• For example, an enzyme known to act in the digestion of foods was named pepsin
and lysozyme was named for its ability to lyse (break down) bacterial cell walls.
others were named for their source: trypsin, named in part from the Greek tryein,
“to wear down,”was obtained by rubbing pancreatic tissue with glycerin.
• Sometimes the same enzyme has two or more names, or two different enzymes
have the same name.
• Because of such ambiguities, as well as the ever-increasing number of newly
discovered enzymes, biochemists, by international agreement, have adopted a
system for naming and classifying enzymes.
• This system divides enzymes into six classes, each with subclasses,
based on the type of reaction catalyzed.
• Each enzyme is assigned a four-part classification number and a
systematic name, which identifies the reaction it catalyzes.
• As an example, the formal systematic name of the enzyme catalyzing
the reaction is ATP:D-hexose 6-phosphotransferase, which indicates
that it catalyzes the transfer of a phosphorylgroup from ATP to
glucose. Its Enzyme Commission number (E.C. number) is 2.7.1.1.
• The first number (2) denotes the class name (transferase); the second
number (7), the subclass (phosphotransferase); the third number (1),
a phosphotransferase with a hydroxyl group as acceptor; and the
fourth number (1), D-glucose as the phosphoryl group acceptor.
• For many enzymes, a trivial name is more frequently used—in this
case, hexokinase.
• International Classification of Enzymes
Class no. Class name Type of reaction catalyzed
1 Oxidoreductases Transfer of electrons (hydride ions or H atoms)
2 Transferases Group transfer reactions
3 Hydrolases Hydrolysis reactions (transfer of functional groups to
water)
4 Lyases Cleavage of C—C, C—O, C—N, or other bonds by
elimination, leaving double bonds or rings, or addition
of groups to double bonds
5 Isomerases Transfer of groups within molecules to yield isomeric
forms
6 Ligases Formation of C—C, C—S, C—O, and C—N bonds by `
condensation reactions coupled to cleavage of ATP
or similar cofactor
