MODULE 8: ENZYMES & METABOLIC PATHWAYS
Metabolism
• is a series of chemical reactions in the body that
converts the food into energy.
• 2 TYPES:
1. Anabolism
2. Catabolism
• Anabolism is powered by catabolism
• Metabolism is the process of converting food
into energy. Therefore, skipping meals may
cause disruption in cellular activities which
may result in sickness.
• Anabolism & Catabolism are both vital
processes
ENZYMES
• Enzymes are molecules that help speed up the
process in a chemical reaction
• Chemical reaction that make up metabolism
do not proceed by themselves.
• Chemical reaction may be switched on and off,
sped up and down depending on the cells'
immediate needs and over all functions.
• Control and regulation of metabolic pathways
are powered by enzymes.
STRUCTURE OF ENZYMES
Active Site
1. Binding Site
 It chooses the substrate active site
2. Catalytic Site
 It performs the catalytic and binds it to action
of enzyme
COMPONENTS OF ENZYMES
1. apoenzyme – protein
• Apoenzyme are called proenzyme when it is
inactive.
1. not attached to any substance
2. enzyme is in its original form
2. cofactor – non – protein
• It is the non protein component which carries
out chemical reactions.
• Cofactors assist apoenzymes
TYPES OF COFACTORS
1. Metal ion activator
• These metals are dietary minerals that are
part of our daily nutritional requirements.
• Without these, some of the body's reaction
may not proceed.
• They bind to apoenzyme temporarily
2. Coenzymes
• Like metal ion activators, they bind to
apoenzyme temporarily.
• They are organic molecule that come from the
vitamins that we take in everyday.
• They are loosely bound organic cofactor
3. Prosthetic cofactors
• Can either be metal ions or organic molecules
• The only difference is that they bind to
apoenzymes permanently.
• They are tightly bound organic cofactor
Enzymes cont'd
• When the apoenzymes and cofactors are
bound, they form an enzyme complex called
HOLOENZYME.
• The holoenzyme now becomes active and
ready for usage.
• Most cofactors can be derived from vitamins
and minerals. It is important, therefore, to
ensure that the basic nutritional needs are met
daily for efficient bodily functions.
• Ultimately, you will see the importance of
enzymes in ensuring that cells are able to
respond to the changing environment
conditions and maximize their efficiency.
ACTIVATION ENERGY
• Typical molecules do not interact with another
unless they are triggered.
• In essence, the presence of energy is vital in
causing reaction to these molecules.
Activation Energy - is the amount of energy required
to stimulate a reaction.
ENZYME SUBSTATE COMPLEX
• Substrates- these are reactants in an
enzymatic reaction
• The substrate combines with an enzyme to
form an enzyme substrate complex:
E + S -----> ES Complex
• Enzymes only catalyze certain reaction.
• Any slight change in shape or condition of the
substrate will stop the enzyme from catalyzing
a chemical reaction.
• The specificity lies on the active site present in
the enzyme.
• Active Sites- are cracks or hollows on the
surface of the enzyme due the manner of
protein folding itself.
• Only molecular substrates that have the
perfect fit can bind to the active sites.
 • It has a lock-and-key relationship. • However some times heat energy can
also increase kinetic energy to a point
• After the reaction is completed, the product is that exceed the energy barrier which
released. results in denaturing of enzymes.
• Then the active site goes back to its original • pH
conditional condition.
• Rate of almost all enzymes catalyzed
SITES OF ENZYME SYNTHESIS reactions depends on pH
• Enzymes are synthesized by ribosomes which • Most enzymes exhibit optimal activity
are attached to the rough endoplasmic at pH value between 5 and 9
reticulum.
• High or low pH value than optimum
• Information for the synthesis of enzyme is value will cause ionization of enzyme
carried by DNA. which result in denaturation of
• Amino acids are bonded together to form enzyme
specific enzyme according to the DNA’s codes • Substrate concentration
substrate enzymes products INHIBITION
• INHIBITORS: Any substance that can diminish
lactose lactase glucose + galactose the velocity of an enzyme catalyzed reaction is
called an inhibitor.
maltose maltase Glucose
• When the enzyme is inhibited, it is not capable
cellulose cellulase Glucose of binding to any substrate.
Examples
lipid lipase Glycerol + fatty acid
Competitive Inhibition:
starch amylase Maltose • Statin drugs such as Lipitor compete with
HMG-CoA(substrate) and inhibit the active
protein protease Peptides + polypeptide site of HMG CoA-REDUCTASE (that bring
about the catalysis of cholesterol synthesis).

LOCK AND KEY MODEL Uncompetitive Inhibition:

- Inhibitor does not compete with substrate
 Proposed by Emil Fischer in 1984.
instead it binds to another site known as
 Lock and key hypothesis assumes the active
allosteric site.
site of an enzymes are rigid in its shape.
 There is no change in the active site before and - Drugs to treat cases of poisoning by methanol
after a chemical reaction. or ethylene Glycol
INDUCED FIT MODEL Irreversible Inhibition:
 More recent studies have revealed that the • The catalytic activity of enzyme is completely
process is much more likely to involved and lost.
induced fit model (proposed by Danial Kosh
Land in 1958) • It can only be restored only by synthesizing
 According to this exposure of an enzyme to molecules.
substrate cause a change in enzyme , which • Aspirin which targets and covalently modifies
causes the active site to change its shape to a key enzyme involved in inflammation is an
allow enzyme and substrate to bind. irreversible inhibitor.
FACTORS AFFECTING RATE OF
ENZYME CATALYZED REACTIONS
• Temperature
• Raising the temperature increases the
rate of enzyme catalyzed reaction by
increasing energy of reacting
molecules.
• Enzymes work maximum over a
particular temperature known as
optimum temperature.
• Enzymes for humans generally exhibit
stability temperature up to 35-45 ᵒC.
 MODULE 9: METABOLIC REACTIONS AND
ENERGY TRANSFORMATION
STRUCTURE OF ATP (ADENOSINE
TRIPHOSPHATE)
ATP Mechanism
 All cells have small storage of highly charged
ATP molecules, specifically located in the
cytoplasm of the cell.
 Energy is transferred when ATP breaks down
into Adenosine Diphosphate ADP
 Breakage of ATP is hydrolysis reaction, a
process of breaking the chemical bonds by
using water.
Functions of ATP
 Chemical work
ATP provides the energy required for
producing complex substances such as
biomolecules.
 Mechanical work
ATP provides the energy for cells and tissues
to perform their function, such as the
circulation of blood, the contraction of
muscles, and pumping of the heart.
 Transport work
ATP provides the energy for substance to
move such exit and entry of compounds
across cell membranes, or substrates binding
to protein enzymes.
Metabolism through ATP
 Heterotrophs obtain ATP through the food
that we eat.
 First, the digestive system breaks down the
ingested food into smaller molecules.
 These smaller units are then absorbed into the
blood stream and transported into the cells.
 The cells use these molecules to convert ADP
molecules into ATP
 If the body does not have this mechanism, it
will easily run out of ATP after a couple of
seconds.
 The higher the metabolism is, the more energy
you can produce and the more fat you can
burn.
ATP from Carbohydrates
 Each time we consume food rich in
carbohydrates, our body replenished and
supplied with more sources of energy.
 Upon intake, carbohydrates are stored in the
muscles as glycogen.
 Glycogen is broken down into glucose, which
will be used in ATP production when the body
needs them, depending on the amount of
physical work to be done.
 Most athletes load themselves up with
carbohydrate-rich foods on the eve before the
competition to store enough glycogen, which
is necessary to facilitate more energy
production during the event.
ATP from Fats
 Fats are great sources of ATP, but most of the
food that we eat contains bad fats instead of
good ones.
 Bad fats are those that are stored immediately
instead of getting used up.
 Because most these bad fats contain high
levels of saturated triglycerides, they may
require high intensity activities for them to
break down.
 Most good fats, on the other hand, have higher
level of unsaturated triglycerides. This makes
them easier to be broken down by the body.
ATP from Oxygen
 Aside from food intake, oxygen is important
for ATP to function well.
 Inhaling deeply through the nose and exhaling
through the mouth will fire up ATP production
and energy release.
 Too many people are shallow breather and do
not even know it. We gulp air while speaking
and eating, essentially starving the cells of
adequate oxygen and fully functioning ATP
molecules, thus, we experience fatigue and
potential weight gain.
CIRCADIAN RHYTHM
 Balance in anabolism and catabolism is
maintained by the circadian rhythm, which
maintains regular or patterned process in the
body within a 24-hour cycle.
 The circadian rhythm is disrupted when an
organism changes certain habits or lifestyles.
Body Mass Index
 Body Mass Index (BMI) is the weight to height
ratio of an individual
Wt in kg
BMI = ----------------
Ht in m2
 STANDARD BMI SCALE
CATEGORY SCALE
Underweight BMI less than 18.5
Normal Weight BMI 18.5 to 24.9
Overweight BMI 25 to 29.9
Obese BMI more than 30

Basal Metabolic Rate

 BMR is the minimum amount of energy,
usually in form of calories, which your body
requires to complete its normal functions.
 It is the amount of calories you need to keep
your cells working.
 If you go below this amount, you may feel
exhaustion, weakness, and sickness because
we are energy deficient.
 Human’s total energy expenditure:
70% - Basal life processes within the tissues
and organs
20% - Physical activities
10 % - Food digestion
FORMULA:
BMR (Female) = 655 + [9.6 x weight (kg) +
[1.8x ht in cm] – [4.7 x age in yrs.]
BMR (Male) = 66 + [13.7 x weight (kg) + [5 x ht
in cm] – [6.8 x age in yrs.]