Enzymes

Enzymes
 Most of the proteins in living cells are the
enzymes.
 It controls the rate of many chemical
reactions to bring about certain metabolic
processes.
 Normal actions of the enzymes are vital
to the well being of the organism.
 Disturbances of enzymes may result to
illness or death.
 Enzymes are protein macromolecules.
◦ They have a defined amino acid sequence, and are
typically 100-500 amino acids long.
◦ They have a defined three-dimensional structure.
 Enzymes are catalysts.
◦ They act as a catalyst to a chemical or
biochemical reaction, with a defined mechanism.
◦ They increase the speed of that reaction, typically
by 106-1014 times faster than the rate of the
uncatalysed reaction.
◦ They are selective for a single substrate.
◦ They speed up rate of reaction by lowering the
activation energy (Ea).
◦ They are stereospecific, meaning the reaction
produces a single product.
Structure of Enzymes
Terms used:

 Substrate
 Competitive Inhibitor
 Reversible Competitive Inhibitor
 The functions of these enzymes are
greatly influenced by the chain structure
of the protein molecule.
 This chain structure may be altered by
breaking peptide bonds. Such a change is
called denaturation, which may be brought
by heat, pressure, acidity, etc. if the effect
is slight, recovery of the broken chain
maybe take place; but if the breakage is
reverse, the change is irreversible.
Enzymes
 Most enzymes end in suffic ─ ase, which
is added to the name of the substrate or
the reaction acted upon. Examples are:
enzymes acting on phosphates are called
reductases.
 Enzymes are capable of acting only on
specific substrate or reactions.
 The activities of the enzymes are
influenced or inhibited by various factors
(temperature, pH concentration of the
enzyme and substrate, and the collision or
contact between the molecules of the
enzymes and substrate.
Enzymes are divided into main groups
according to chemical reactions they
perform. They are as follows:
 Oxidoreductase
– bring out oxidation-reduction
reactions. These reactions involve the
transfer of electrons from one molecule
(the reductant) to another (the oxidant).
These reactions are vital to life for their
role in essential metabolic processes like
glycolysis, which occurs in nearly every
organism on the planet.
 Transferases
– affect the transfer of group. The
transferase enzymes catalyze the
transfer of a functional group (such as
methyl) from one molecule to another.
The first molecule is called the donor
and the second molecule is called the
acceptor. These transfer processes are
some of the most basic and vital
reactions in life.
 Hydrolases
– influence hydrolytic reactions. The
hydrolases bring about hydrolysis: this is
the breaking of chemical bonds with the
addition water. There is a wide variety of
identified hydrolases, over 200 of them,
from those that break down proteins to
those that cleave ester bonds and more.
Exohydrolase enzymes cut the molecules
at the end of the chain, and
endohydrolase enzymes do so in the
middle of the chain.
 Lyases
– bring about the addition or removal of
a group to and from double bonds. Lysis
reactions – those that generate a double
bond – are brought about by lyase enzymes.
Lysis reactions are the kind of elimination
reactions that are not hydrolytic or
oxidative. The lyases are also sometimes
called synthase enzymes. A Michael addition
– the reverse reaction – is also possible.
However, two substrates are required for
the reverse reaction to happen, whereas one
substrate is required for the lysis reaction.
This makes lyases unique among enzymes.
 Isomerases
– catalyze isomerization process. The
isomerase enzymes catalyze structural
changes within a molecule – this just
brings about a change in shape since there
is only one substrate and one product
with nothing gained or lost. Within this
category, there are a few sub-categories
depending upon their effect. There are
geometric, structural, enantiomer, and
stereoisomer isomerases.
 Ligases – or synthetases – combine two
or more molecules by splitting the
phosphate bonds. Ligation is brought
about by ligase enzymes. Ligation occurs
when two substrates are joined together.
Chemical potential energy is usually
required for this reaction to occur, so it is
often paired with the hydrolysis of a
diphosphate bond. DNA ligase – which
catalyzes the ligation or repair of breaks
in DNA – is an example of a vital enzyme
in this category.
 Works together in metabolic pathways.
* A metabolic pathway is a sequence of
chemical reactions occurring in a cell.
 Many enzymes are assisted by chemical
substances called cofactors which may be
ions or molecules. These factors are
required for a chemical reaction to take
place. (Example: Iron, Manganese, and zinc)
 Organic molecules, acting as cofactors are
called coenzymes (Examples: NAD and
FAD)
When an enzyme functions, a key portion
of the enzyme called “active site”
interacts with the substrate. After the
interaction, a change in shape in the active
site places stress on the substrate. This
physical stress aids the alteration of the
substrate and produces the end product.
The combination when the active site
interacts with the substrate is referred to
as enzyme-substrate complex. After
the enzyme has performed its work, the
product/s drift away. The enzyme is free
to function in another chemical reaction.
There are two metabolic pathways
namely:
 Catabolic pathways – involved the
breakdown or digestion of large complex
molecules. General term is Catabolism.
 Anabolic pathways – involve the synthesis
of larger molecules, generally by joining
smaller molecules together. General term
is Anabolism.
 Anabolism is the constructive phase that
requires energy while Catabolism is the
destructive phase that releases energy.
 Primarily, energy is derived from sunlight. In
the process of photosynthesis, green plants
capture the radiant energy to produce
energy-rich organic molecules. The chemical
energy found in organic molecules
represents potential energy some of which
are utilized by the plants themselves. The
energy needed by animals is obtained either
directly or indirectly from plants.
Based on the mechanism of extracting energy
from their own metabolism, cells and
organisms are grouped into the following:
1. Autotrophic (green plants) – transform
CO2 and H20 into organic molecules
through photosynthesis.
2. Heterotrophic (animals) – obtain energy
from different foodstuffs by autotrophic
organisms. Heterotrophic nutrition maybe
holozoic (by digestion), saphrophytic or
parasitic. Energy in the organic molecules is
released in respiration.
In cells of living animals are complex
systems of chemical reactions to convert
energy from one type to another form.
The chemical energy of organic molecules
is transformed into useful potential
energy of energy-rich phosphate
compounds, the adenosine triphosphate
(ATP). This potential energy is converted
to kinetic energy utilized by the cells to
do work. The energy finally passes to the
environment as heat energy.
Transformation of energy takes place in the
process of cellular respiration, which
involves an orderly series of the enzymes-
controlled chemical reactions. The
chemical bonds of the organic molecules
are broken and the energy is gradually
released from each reaction, which is
controlled by specific enzyme.