Enzymes are proteins that increase the rate of reaction by lowering the energy of activation.

They
catalyze nearly all the chemical reactions taking place in the cells of the body. An enzyme is a
type of protein that acts as a biological catalyst, facilitating and speeding up chemical reactions
in living organisms. Enzymes come from a Greek word “enzymos” are the chemical catalysts of
biological system. Enzymes have extraordinary catalytic power, often far greater than that of
synthetic or inorganic catalysts.
Enzymes also apply in our day to day life’s (real world), they have numerous practical
applications across various fields: Biotechnology: enzymes are used in genetic engineering to
manipulate DNA, in the production of biofuels, and in the synthesis of pharmaceuticals. Food
industry enzymes are employed in food processing and production, such as in the fermentation of
cheese, brewing of beer, and clarification of fruit juices. Diagnosis: enzyme-linked
immunosorbent assay (ELISA) is a widely used diagnosis technique that relies on enzyme
activity to detect specific molecules in biological samples. Textile industry: enzymes are used in
the finishing of textiles to improve the textures and appearance of fabrics. Medical field;
enzymes replacement therapies are used to treat genetic disorders like phenylketonuria (PKU)
and Gautier’s disease
The molecules upon which enzymes may act are called substrates into different molecules
known as products. Enzymes play essential in various metabolic processes, breaking down or
building up molecules within cells .Almost all metabolic processes in the order to occur at rates
fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual
steps. Enzymes work by lowering the activation energy required for a chemical reaction reaction-
rate. Enzymes are highly specific, each one typically catalyzing a particular chemical reaction or
group of related reactions. The study of enzymes is called enzymology and the field of
pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to
carry out biological catalysis, which is often reflected in their amino acid sequences and unusual
‘pseudocatalytic’ properties.
Like all catalysts, enzymes increase the reaction rate by lowering its activation energy. Some
enzymes’ can make their conversion of substrate to product occur many millions of times faster.
An extreme example is orotidine 5`-phosphate decarboxylase, which allows a reaction that
would otherwise take millions of years to occur in milliseconds .Chemically enzymes are like
any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a
reaction .Enzymes differ from most other catalysts by being much more specific. Enzymes
activity can be affected by other molecules: inhibitors are molecules that decrease enzyme
activity, and activators are molecules that increase activity, and activators are molecules that
increase activity. Many therapeutic drugs and poisons are enzymes inhibitors. An enzymes
activity decreases markedly outside its optimal temperature am PH, and many enzymes are
(permanently) denatured when exposed to excessive heat, losing their structure and catalytic
properties.
Enzymes are remarkable biological molecules that play a vital role in the functioning of all living
organisms. They are often referred to as “nature’s catalysts” because of their ability to accelerate
chemical reactions within cells without being consumed in the process. Enzymes are essential for
life as well as we know it, as they control and regulate a wide array of biochemical reactions,
from digestion to DNA replication. In this document, we will delve into the structure, types, and
functions of enzymes, shedding light on their pivotal role in the world of biology.
STRUCTURE OF ENZYMES AND THE LOCK AND KEY HYPOTHESIS
Enzymes are proteins comprised of amino acids linked together in one or more polypeptide
chains. This sequence of amino acids in a polypeptide chain is called the primary structure. This,
in, turn, determines the three-dimensional structure of the enzymes, including the shape of the
active site. Enzymes are typically protein, although some RNA molecules, known as ribozymes,
also exhibit enzymatic activity. The structure of an enzyme is intricately linked to its function.
Enzymes are large, complex molecules composed of amino acids, which are linked together in a
specific sequence to form a specific sequence to form a polypeptide chain. The unique three-
dimensional shape dimensional shape of this chain, known as the enzyme’s tertiary structure,
determines its catalytic activity. The key structures of enzymes include: Active site: this is the
region of the enzyme where the substrate (s), the molecules upon which the enzyme’s acts, bind.
Substrate-binding site: enzymes often have one or more substrate-binding sites in addition to the
active site, which can influence substrate specificity and enzyme function. Cofactors and
coenzymes some enzymes require non-protein molecules, called cofactors or coenzymes, to
function properly. These molecules assist in catalysis by aiding in chemical reactions.
Quaternary structure; some enzymes are composed of multiple subunits, each contributing to the
overall structure and function of the enzymes.

LOCK AND KEY HYPOTHESIS

In 1894, German chemist Emil Fischer proposed the lock and key theory, which states that the
enzymes active site and the shape of the substrate molecules are complementary to one another.
In the lock and key model action: the active site has a rigid shape, only substrates with the
matching shape can fit, the substrate is a key that fits the lock of the active site.
Enzyme as a lock: enzyme is likened to a lock with a specific shape, represented by the enzyme’s
active site. The active site is a region on the enzymes surface with a unique three-dimensional
structure. Substrate as a key: the substrate compared to a key that fits perfectly into the active site
of the enzyme. Just as a key must have the right shape to fit into a lock, a substrate must have a
complementary shape to interact with the enzymes active site. Specificity: one of the key
principles of the lock and key theory is the idea of specificity. Each enzyme has an active site
that is precisely shaped to accommodate a particular substrate or a group of closely related
substrates. This ensures that enzymes are highly selective and only interact with specific
molecules. Catalysts: when the substrate (key) binds, it forms an enzyme substrate complex. This
complex is highly unstable and prone to undergoing a chemical reaction. The enzyme catalyses’
this reaction, facilitating the conversion of the substrate into products while remaining
unchanged itself.
The lock and key theory contains some limitations. Rigidity and specificity; One of the main
limitations of the lock and key theory is its assumptions of rigidity. This model implies that the
enzymes active site is a static structure with a fixed shape that perfectly matches the substrate. In
reality, enzymes are more dynamic than this model suggests. Many enzymes can accommodate
substrates with slight structural variation through induced-fit mechanisms. The lock and key
theory does not account for the conformational changes that enzymes’ can undergo upon
substrate binding, which are crucial for understanding their catalytic efficiency.
Doesn’t explain all enzyme-substrate interactions: enzymes often exhibit a degree of flexibility
in their active sites. This flexibility allows them to adjust their shape to better accommodate
substrates, even if the fit is not perfect. This phenomenon is better explained by the induced-fit
model, proposed as an alternative to the lock and key theory. In the induced-fit mode, the
enzymes active site undergoes changes in shape and conformation upon substrate binding,
highlighting the dynamic nature of enzyme-substrate interactions.

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 CATEGORIES OF ENZYMES
Enzymes can be classified into 7 categories according to the types of reaction they catalyse.
These categories are oxidoreductases, hydrolases, transferases, lyases, isomerases, ligases, and
translocases, out of these, oxidoreductases, transferases and hydrolases are the most abundant
forms of enzymes. Oxidoreductases; these enzymes catalyze oxidation reduction reactions,
transferring electrons between molecules. Examples include dehydrogenases and oxidases.
Transferases: transferases catalyze the transfer of functional groups, such as phosphate or methyl
groups, from one molecule to another. Kinases, for instance, transfer phosphate groups.
Hydrolases: hydrolases facilitate the hydrolysis of chemical bonds by adding water molecules.
Lipases, amylases, and proteases are examples of hydrolases.
Lysases: lysases cleave chemical bonds without the addition of water e.g. aldolase (an enzyme
in glycolysis) catalyzes’ the splitting of fructose-1-6-biphosphate to glycraldehyde-3-phoshate
and dihydroxyacetone phosphate. Ligases; these catalyze the association of the two molecules.
For example, They are also known as synthetases, join two molecules together using energy from
ATP.DNA ligase, involved in DNA replication, is a well-known example. DNA ligase catalyze
the joining of the two fragments of DNA by forming a phosphodiester bond. Isomerases; these
catalyze the formation of an isomer of a compound and the example phoshphoglucomutase
catalyzes the conversion of glucose-1-phospate to glucose-6-phosphate (phosphate group is
transferred from one to another position in the same compound) in glcogenolysis9glycogen is
converted to glucose for energy to be released quickly). Enzymes like isomersases are vital in
metabolic pathways.
Translocases; this is a general protein that assisting moving another molecule, usually across a
cell membrane. These enzymes catalyze the movement of ions or molecules across membranes
or their separation within membranes or their separation within membranes. The reaction is
designated as a transfer from “side 1” to side 2” because the designations “in” and “out”, which
had previously been used, can be ambiguous.Transocases are the most common secretion system
in gram positive bacteria.
COFACTORS OF ENZYMES
A cofactor is a non-protein chemical compound that is bound (either tightly or loosely) to an
enzyme and is required for catalysis. These molecules are crucial for the play of specific roles in
facilitating enzyme-substrate interactions and promoting reactions rates. Coenzymes are organic
molecules, often derived from vitamins. There are two types of cofactors: coenzyme: The non-
protein component, loosely bound to coenzymes by non-covalent bound. Example vitamins or
compound derived from vitamins. Prosthetic groups; the non-protein components, tightly bound
to the Apo enzyme by covalent bounds is called a prosthetic group. One important groups of
coenzymes is the vitamin-derived coenzymes. For instance, niotinammide adenine dinucleotide
(NAD+) and flavin adenine dinucleotide (FAD) are coenzymes derived from vitamins B3 and
B2, Respectively. These coenzymes act as electron carriers during redox reactions. They accept
electrons from substrates and transfer of electrons, such as those in cellular respiration.
PRACTICAL APPLICATIONS OF ENZYMES
Enzymes play an important role in metabolism, diagnosis, and therapeutics. All biochemical
reactions are enzyme catalyzes in the living organisms. Level of enzymes in the blood are of
diagnostic importance e.g. it is a good indicator in diseases such as myocardial infarction.
Enzymes can be used therapeutically such as digestive enzymes. Enzymes have multiple
functions in living organisms their functions can be summarized as follows; Catalysis: enzymes
increase the rate of chemical reactions by lowering the activation energy required for the reaction
to occur. This enables vital processes like digestion, respiration, and DNA replication to proceed
at biologically relevant rates. Specificity: enzymes are highly specific in their action. Each
enzymes typically acts on a particular substrate and this specificity is crucial for maintaining
order in complex biochemical pathways.
Regulation: cells regulate activity to ensure that biochemical processes occur at the right time
and in the right amounts. This regulation can be achieved through factors like allosteric
modulation and feedback inhibition. Metabolism: enzymes are integral to metabolism pathways,
where they facilitate the conversion of one molecule into another. For example, enzymes like
glucose-6-phosphatase are crucial in glucose metabolism. Digestion: in the digestion system,
enzymes like amylase, lipase, and protease break down complex food molecules to simpler
forms that can be absorbed by the body. DNA replication and repair: enzymes like DNA
polymerase and DNA ligase are vital for DNA replication and repair, ensuring the faithful
transmission of genetic information.
FACTORAS AFFECTING ENZYME ACTIVITES
The activities of enzymes can be affected by different factors. Below are some of the factors that
can affect enzyme activities; Temperature: enzymes have an optimal temperature at which they
function most efficiently. Extremes of temperature can denature enzymes, rendering them
inactive. PH: enzymes also have an optimal PH at which they operate. Changes in pH at which
they operate. Changes in PH can disrupts the enzymes active site and affect its function.
Substrate concentration: the rate of an enzyme catalyzed reaction increases reaction increases
with increasing substrate concentration until the enzyme becomes saturated, at which point
further increases in substrate do not affect the reaction rate.
Cofactors and coenzymes: enzymes activity may depend on the presence of specific cofactors or
coenzymes. For example, the enzyme catalase requires iron as a cofactor. Inhibitors enzymes
activity can be inhibited by molecules known as inhibitors. Competitive inhibitors compete with
the substrate for binding to the active site, while non-competitive inhibitors bind elsewhere on
the enzyme, altering its conformation. Environmental conditions; Extreme temperature are the
most dangerous, high temperatures may denature (unfold) the enzyme, PH (most 6-8pH near
neutral) and substrate concentration. The environmental conditions involve optimum
temperature; which is the temperature at which the enzymatic reaction occurs faster.PH also
affects the rate of enzyme substrate complexes, most enzymes have an optimum pH around 7
(neutral), however, some prefer acidic or basic conditions.
CONCLUSION
Enzymes play a crucial role in the complex biological machinery of life as the elegant designers
of several biological proceses.it is impossible to overestimate their importance because they are
the catalysts for biological processes, the watchdogs of metabolic pathways, and the conductors
of molecular symphonies. The astonishing functions of enzymes, the mysteries buried inside
their structures, and their extensive influence on biology, technology, and medicine are all
brought to mind as we draw to a close our investigation of enzymes. The biological catalysts that
power life’s key chemical changes are known as enzymes. They allow processes to move
forward with astounding efficiency by decreasing activation energy barriers. No matter if it’s the
breakdown of nutrients during digestion, DNA replication, or creation.

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