ENZYMES

Definition
• Enzymes are biocatalysts.
• Enzymes are catalysts for biochemical reactions in
living cells.
• Enzymes help to speed up reactions of digestion
and metabolism.
• The term enzyme was derived from Greek means
“in yeast” because the yeast cells were the first to
reveal enzyme activity in living organisms.
• It was first introduced by W. Kuhne in 1878. The
study of enzymes is known as enzymology.
• Enzymes are located in the cells, cytoplasm
mitochondria, tissues and body fluids.
• Endoenzymes
Most of the enzymes function within the cells.
These enzymes are called endoenzymes.
E.g. Metabolic enzymes
• Exoenzymes
Some enzymes are liberated by living cells
and catalyze vital reactions outside the cell.
These are called exoenzymes.
e.g. Digestive enzymes (amylase, lipase, protease)
 Properties of enzymes
• They are proteins.
• They are soluble and colloidal in nature.
• Enzymes are catalysts.
• Remain unaltered in the end.
• Required in small quantities
• Effect of temperature
• Reversibility of enzyme action
• Specificity of enzyme
 Enzymes are proteins
Most of the enzymes are simple or conjugated proteins.
They exhibit all the properties of proteins.
Colloids
• Enzymes are colloidal in nature.
Denaturation
Denaturation is the change in structure and loss of
activity
Enzymes are subject to denaturation by changes in pH or
increase in the temperature.
Enzymes are catalysts
Enzymes accelerate the speed of reactions.
Remain unaltered in the end.
The enzyme promotes a given reaction, but
itself remains unchanged at the end of reaction.
Required in small quantities
Only a small amount of enzyme is required by a
biological system for a complete reaction.
A simple enzyme can act upon 5lakhs substrate
molecules per minute. This value is known as turn
over number.
The number of substrate molecules catalyzed by
an enzyme is called turn over number.
 Effect of temperature
• Enzymes are sensitive to heat.
• They are destroyed by high temperature.
• Above 60 degree celsius the enzyme coagulate and become
inactivated.
• Every enzyme has an optimum temperature at which the
rate of activity is maximum.
• The enzyme is most active at the optimum temperature
• The optimum temperature ranges between 30 and 40℃ for
most of the enzymes.
• The optimum temperature for catalyze is 30℃.
• The rate of activity decreases when the temperature goes up
or goes down from the optimum temperature.
The activity of the enzyme steadily increases
when the temperature is raised to the
optimum level.
The reaction velocity doubles for every rise
in 10℃. This is called Q10 or temperature co
efficient or temperature quotient.
 Reversibility of enzyme action
• Most of the enzymes are characterized by the
reversibility of their actions.
• The enzymes act in either directions

• The same Phosphoglucomutase enzyme converts

glucose 6 phosphate into glucose 1 phosphate
 Specificity of the enzyme
• Each enzyme will react with only one type of
substrate or a group of related substrates. This
property of enzyme is called specificity of
enzymes.
• According to the degree of specificity classified
into four types.
• Absolute specificity
• Group specificity
• Linkage specificity
• Stereo chemical specificity
Absolute specificity
When an enzyme acts on only one
substrate that is called absolute specificity
E.g. Urease acts only on urea
Lactase acts only on lactose.
Group specificity
A particular enzyme acts only on a
particular chemical group.
E.g. Glycosidase acts on glycosides
Trypsin acts on peptide bonds
• Linkage specificity
The enzyme will act on a particular type of
chemical bond regardless of the rest of the
molecular structure.
Stereo chemical specificity
The enzyme will acts only one of a pair of
optical isomers.
E.g. D amino acid oxidase oxidises D amino acids.
L amino acid oxidase oxidises L amino acids and not
D amino acids. D and L aminoacids refer to the
position of NH3 groups to the right or left of the
carboxyl group respectively.
Chemical nature of enzymes and nomenclature
 Simple Enzymes
• Some enzymes are simple proteins, i.e., on
hydrolysis, they yield amino acids only.

• Digestive enzymes such as pepsin, trypsin and

chymotrypsin are of this nature.
 Conjugate Enzymes
• It is an enzyme which is formed of two parts – a protein
part called apoenzyme (e.g., flavoprotein) and a non-
protein part named cofactor.
• The complete conjugate enzyme, consisting of an
apoenzyme and a cofactor, is called holoenzyme. T
• here can be an enzymatic activity only when both
components (apoenzyme and cofactor) are present
together.
• The cofactor is sometimes a simple divalent metallic ion
(e.g. Ca++, Mg++, Zn++, Co++, etc.), and sometimes a
nonprotein organic compound.
• However, some enzymes require both kinds of cofactors.
• If the cofactor is firmly bound to the apoenzyme, it is
called prosthetic group.
 Metallo-enzymes
• The metal cofactors involved in enzymic
reactions are both monovalent (K+ ) and
divalent cations (Mg++, Mn++, Cu++).
• These may be loosely held by the enzyme, or
as in some cases, go into the composition of
the molecule itself.
• If the metal forms part of the molecule, as
iron of haemoglobin or cytochrome, the
enzymes are called metallo-enzymes.
 Isoenzymes (Isozymes)
• At one time it was believed that an organism
has only a single enzyme for a given step of a
metabolic reaction.
• It was later discovered that a substrate may be
acted upon by a number of variants of an
enzyme producing the same product.
 Nomenclature of enzymes

• The naming of enzymes is called

nomenclature of enzymes.
• Enzymes are named based on the substrates,
the reaction, synthesis, chemical nature, etc.
Nomenclature based on the substrate
• Substrate is the substance on which an enzyme acts.
• Many enzymes are named by adding the suffix ase to
the name of substrate.
• The enzymes acting on proteins are named as
proteinases.
• The enzymes acting on lipids are named as lipases.
• The enzymes acting on nucleic acids are named as
nucleases.
• The enzyme acting on maltose is maltase.
• The enzyme acting on lactose is lactase.
• The enzyme acting on sucrose is sucrase
• The enzyme acting on urea is urease.
 Nomenclature based on reaction
• Some enzymes are named by adding the suffix “ase”
to the reaction.
• The enzyme catalysing reduction is reductase.
• The enzyme catalysing dehydrogenation is
dehydrogenase.
• The enzyme catalyzing phosphorylation is
phosphorylase
• The enzyme catalysing transaminaton is
transaminase.
• The enzyme catalysing isomerization is isomerase.
 Based on substrate and reaction
• Some enzymes are named based on the
substrate and the type of reaction.
• The enzyme removing carbon di oxide from
pyruvic acid is named as pyruvic decarboxylase.
• The enzyme removing hydrogen from isocitric
acid is named as isocitric dehydrogenase.
 Based on synthesis

• Enzymes are also named by adding the suffix

“ase” to the substance to be synthesized.
• The enzyme synthesizing citric acid is named
as citric synthetase.
Classification of enzymes
 Based on discoverer
• Certain enzymes are named by the discoverers of enzymes.
E.g. Pepsin, Trypsin etc.
Based on enzyme commission
• Commission on enzymes named the enzymes into 6 groups
based on the chemical reaction catalyzed. They are
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
Oxidoreductases
The enzyme catalyzing oxidation – reduction
reaction are named as oxidoreductases. The
important subclasses are
E.g. Oxidases, Oxygenases, dehydrogenases.

Dehydrogenases are enzymes that catalyze the

removal of hydrogen from one substrate and
pass it on to second substrate.
Transferases
The enzymes which catalyze the transfer
of a group between two substances are also
called transferases.
e.g. Transaminase transfers amino group from
one aminoacid to another.
• Hydrolases
The enzymes which catalyze the substrates
by adding water across the bond they split are
called hydrolases.
E.g. Proteases, esterases, carbohydrases.
Lyases
The enzymes which remove the groups from
substrates by mechanisms other than
hydrolysis are named as lyases.
e.g. Aldolase, enolase, fumarase etc.
Ligases
• The enzymes which link two substrates are called ligases. They
are also called synthetases
• E.g. Acetyl CoA Synthetase
Glutamine synthetase
Isomerases
Isomerases catalyze the interconversion of a compound to one of
its isomers.
These enzymes catalyze intermolecular rearrangements. The
phosphohexose isomerase catalyses the following
interconversion
Co enzyme and Prosthetic groups
 Co enzyme
• In the co enzyme the co factor component is
not firmly attached to the enzyme protein.
• Here the co factor exist in free state in the
solution.
• It makes a contact with the enzyme protein
only at the instant of enzyme action.
• E.g. NADH, FADH, CoA
 Prosthetic groups
• In the co factor component is firmly attached
to the enzyme protein.
 Enzyme Inhibition
• The inactivation of enzymes is called enzyme
inhibition.
• The substances inactivating enzymes are
called enzyme inhibitors.
• There are three types of enzymes
Competitive inhibition
Non competitive inhibition
Allosteric inhibition
 Competitive inhibition
• It is a reversible enzyme inactivation.
• The substrate bringing about reversible
inactivation is called competitive inhibition.
• The competitive inhibitor closely resembles
the substrate.
• So it can complete with the substrate to attach
with the active site of the enzyme.
• It combines with the active site of the enzyme
to form enzyme inhibitor complex.
 The competitive inhibition is characterized by the following
features

• Lack of absolute specificity of an enzyme

towards a substrate.
• Structural similarity between substrate and
enzyme inhibitor.
• Affinity of the enzyme is more for the inhibitor
than for the substrate.
• Inhibition is reversed by increasing the
concentration of substrate.
• Melonic acid and glutaric acid are the
inhibitors of succinic dehyrogenase.
• succinic dehyrogenase cataltzes succinic acid
into fumaric acid.
• Sometimes succinic dehydrogenase is
inhibited by melanic acid and glutaric acid.
• Because melanic acid and glutaric acid are
very simiilar to succinic acid in structure.
• The amount of inhibition in this type of
reaction is related to
• Inhibitor concentration
• Substrate concentration
• Relative affinity of inhibitor and substrate
• The inhibitory effect is reversible