G-11 PPT P-2
G-11 PPT P-2
G-11 PPT P-2
Figure: Anatomy of a hexapod insect, note that insects have a developed digestive system
(yellow), a respiratory system (blue), a circulatory system (red), and a nervous system (red).
2.3.4 Reproduction in Frog
Figure: Crops destroyed by desert locusts (left) and other insects (middle and right)
Cont…
Moreover, several insects serve as vectors for transmitting diseases
from one organism to another or serve as intermediate hosts for
several pathogens and transfer disease from one to another.
For example, Anopheles mosquitoes transfer malarial parasites,
“Plasmodium,” from one person to another.
Culex mosquitos spread filariasis and transmit filarial worms from
infected to healthy people.
The tsetse fly, Trypanosoma gambiense, also spreads the African
sleeping sickness to the human population.
The housefly (Musca domestica) spreads food and water-borne
diseases to human populations.
2.5 Animal Behavior
• Animal behavior means all the ways in which animals interact with
other organisms and the physical environment.
ETHOLOGY: The study of animal behavior with emphasis on the
behavioral patterns that occur in natural environments.
• It includes the movements of animals, interaction of animals within
and with the environment and learning about their environment.
2.5.1 Types of Animal Behavior
• Animal behavior can be categorized into two main types:
1. innate or inherent behavior: Nature/innate, genes determine behavior
2. learned or acquired behavior:Nurture/ learned, Experience and
learning determine behavior
1. Innate or inherent behavior
Innate or inherent behavior is an inborn behavior that is determined by
genes and independent of experience and specific to a species.
Innate means „inborn‟.
Innate behavior is A behavior that is present at birth or hatching.
They don‟t have to be learned.
There are three types of innate or inherent behavior, and these are
instinctive, reflexive, and orientative.
An instinct is a complex pattern of innate behavior.
The following examples are instinctive behaviours in animals.
@ Web making in spiders @ Nest-building in birds
@ Swimming with dolphins and other aquatic species.
@ Opening of mouth in chicks of many bird species when their
mother returns to the nest.
@ Honeybees dance when they return to the hive after finding a
source of food.
Cont…
Reflex action
Reflexes the simplest innate behaviors are reflex actions.
A reflex is a sudden, an automatic, involuntary response to
stimuli.
It does not involve a message from the brain.
During a reflex action, messages about pain do not travel all
the way to and from the brain.
Instead, they travel only as far as the spinal cord, and the
spinal cord responds to the messages by giving orders to the
muscles.
This allows you to respond to pain more quickly.
The following examples are reflex behaviours in animals.
@ Touch a sharp or hot object: you pull your hand away rapidly without
even thinking about
@ blinking: when something gets too close to your eye & you close your
eyes
• Orientational behaviour
Orientation in its simplest sense means taking up a particular bearing (e.g. due
south) with respect to the current position, regardless of destination.
Taxis: is directed in relation to a given stimulus.
It is the orientation of an animal (directed either towards or away) in response to
the source of stimulus. If the orientation is towards the stimulus, it is called as a
positive taxis, and if it is away from the stimulus, it is known as a negative taxis.
Example: The movement of cockroaches away from the source of light. Kinesis is
undirected, random movement.
Kinesis: is a type of locomotory behavior in relation to the source of stimulus.
The animal responds to the variation in the intensity of the stimulus and not the
source or direction of the stimulus.
Example: The movement of woodlice in relation to the temperature around them.
Question
• What is the difference between phototaxis,
• chemotaxis, thigmotaxis and geotaxis? Explain with
2. Learned or acquired behavior
Learned or acquired behavior is not inherited and not determined
by genes.
It is acquired through practice or a specific experience with an
external event
It is the type of animal behavior acquired during the lifetime of
an individual.
It allows an individual organism to adapt to changes in the
environment that are modified by previous experiences.
Learned behavior develops during an animal‟s lifetime.
It is modified by experience is called trial-and-err or learning.
Examples of simple learned behavior include
Non-associative learning Habituation, sensitization
Classical conditioning, operant conditioning, latent and insight
learning
Habituation
Habituation is a simple form of learning in which an animal
stops responding to a stimulus, or cue, after a period of repeated
exposure.
It is loss of responsiveness to stimuli that convey little or no
information
Animals learn not to respond to repeated occurrences of
stimulus
This is a form of non-associative learning, in which the
stimulus is not linked with any punishment or reward.
E.g. The animal learns not to respond to irrelevant stimuli such
as movements due to wind, cloud, shadows, wave action etc
For example, you were reading a book when someone turned on
the television in the same room. At first, the sound of the
television might have been annoying. After a while, you may no
longer have it noticed. Accordingly, it mean that you have
become accustomed to the sound.
Sensitization
It is the opposite of habituation in that repeated
presentations of the stimulus cause an increase in
response.
Sensitization, also referred to as reverse tolerance, is a
non-associative learning process in which repeated
administration of a stimulus results in the progressive
amplification of a response.
It occurs when a stimulus is presented above the
tolerance threshold.
For example, repetition of a painful stimulus may
make one more sensitive to a loud noise.
The stimulus has to be unpleasant or aversive
In farm animals, increased responsiveness follows a
reward or punishment (or 'reinforcement') mainly
associated with predator, food and mates
Classical conditioning
It is a result of associative learning in which a response already associated with one
stimulus is associated with a second stimulus to which it had no previous
connection.
A stimulus is substituted for one that is already associated with a behavior
Animal learns to associate the new stimulus with the reward. Arbitrary stimulus
associated with a particular outcome
It is passive
Classical conditioning was discovered by Ivan P. Pavlov, a Russian physiologist.
There are three stages of classical conditioning. Stages:
Stage1: Before conditioning: unconditioned stimulus (UCS) produces an
unconditioned response (UCR) in an individual, which means that a stimulus in the
environment has produced a behavior or response which is unlearned (i.e.,
unconditioned), and therefore it is a natural response which has not been taught. In
this case, no new behavior has been learned yet.
Stage 2: During conditioning: During this stage, a stimulus that produces no
response is associated with the unconditioned stimulus, due to what it is known as a
conditioned stimulus (CS). For learning to take place, the UCS must be associated
with CS on a number of occasions, or trials at this stage.
Stage 3: After conditioning. This conditioning happens once the conditioned
stimulus (CS) has been associated with the unconditioned stimulus (UCS) to create a
new conditioned response.
A stimulus is substituted for one that is already associated with a
behavior
Animal learns to associate the new stimulus with the reward. Arbitrary
stimulus associated with a particular outcome. It is passive
The reward follows the stimulus
Ivan P. Pavlov a Russian scientist introduces a new stimulus before
the usual stimulus.
Ivan P. Pavlov performed experiments using this type of conditioning.
He knew that the sight and smell of food made hungry dogs secrete
saliva.
Operant conditioning
Operant conditioning is a type of associative learning in which an
animal learns to associate one of its behaviors with a reward or
punishment
The animal must perform the behavior in response to a stimulus to
get the reward
Unlike classical conditioning, the reward follows the behavior,
not the stimulus
• Operant conditioning is a result of associative learning in which a
bit different from classical conditioning because it does not rely on
an existing stimulus-response pair.
• It was discovered by B.F. Skinner. Based on thetheory of operant
conditioning, behavior willlikely be repeated when the organism is
reinforced (rewarded), and behavior will occur less frequently
when it is punished.
• Skinner identified three types of responses or operant behavior.
• Operant conditioning allows animals to learn behaviors to receive
a reward or avoid punishment
• Reward strengthens the correct response
• Reinforcers: Increase the probability of a behaviour being repeated,
are positive or negative make response more likely in the future
• Punisher: whether positive or negative make response less likely in
the future.
• It decreases the likelihood of a behaviour being repeated.
• Neutral operants: are responses from the environment that neither
increase nor decrease the probability of a behavior being repeated.
D. Insight learning : Problem Solving
Highest form of learning (does not result from immediate
trial-and-error learning)
Based on advanced perceptual abilities such as thought and
reasoning from information previously learned
Insight learning is problem solving without trial and error
It is sudden problem solving without prior experience
It may involve mentally manipulating concepts to arrive at a
solution
Problem solving is the process of devising a strategy to
overcome an obstacle
For example, chimpanzees can stack boxes in order to reach
suspended food
It is the ability to do something right the first time with no
prior experience
It requires reasoning ability–the skill to look at a problem
and come up with an appropriate solution
Insight is the most complex kind of learning
Animal uses previous experience to respond to new situation
E.g.: Solving math problems
Figure: Chimpanzees may use insight to solve problems.
4. Inflexible Flexible
(stereotype patterns
of behaviour)
2.5.2 Patterns of Behavior
There are different behavioral patterns in animals.
The behavioral patterns are different due to the diversity
of species.
There are also common patterns of behavior exhibited by
many species.
Examples of behavioral patterns in animals include:
Behavioral cycles Reproductive behavior
Social behavior Competition
Territory and communication.
Behavioral cycles or biological clocks
Behavioral cycles are pattern in which animals respond to
periodic changes in the environment.
i. Daily or Circadian rhythms:(sleep and wake)
Circadian rhythms, are 24-hour cycles that are part of the body‟s
internal clock, running in the background to carry out essential
functions and processes.
One of the most important and well-known circadian rhythms is the
sleep-wake cycle.
Location of the clock
– Suprachiasmatic nucleus of the
hypothalamus
– Pineal gland- Secretes Melatonin
promotes sleepfulness
ii. Circalunar (circamonthly) Cycles
A circalunar cycle is about 29 days long (one lunar month).
Because the position of the moon and sun generate tidal
patterns, they can affect marine organisms
iii. Circaannual Cycles or seasonal cycles.
A circaannual cycle is about 365 days long (one year)
For example seasonal migration (movement).
Seasonal migration refers to the movement of various
species of birds, insects, and mammals from one
habitat to another during different times of the year
because of seasonal fluctuations in factors such as the
availability of food, sunlight, temperature, and
breeding difficulty.
Example: migration of various whale and bird species
from their summer habitats in the Arctic or Antarctic
to the tropical waters near the equator and warmer
latitudes, respectively.
Social behaviour
Social behaviour: it is the behavioral pattern of animals
commonly observed in that live in groups.
Insects such as ants, termites, bees, exhibit some of the
most well developed social behavior and wasps are social
behaviors.
One benefit of social behavior for these insects is that
different individuals perform better in certain activities or
division of labor as workers and soldiers.
Other examples
• of social behaviour are observed in elephants, penguins,
• human beings and other primates
Eusociality
2. Homoeothermic Animals
Homoeothermic or endothermic animals are those animals that
having constant and relatively high body temperature.
They can generate internal heat to maintain a constant internal
body temperature.
Their cellular processes operate optimally even when the
environment is cold and loses heat when the environment is hot.
They use morphological, physiological and behavioral methods
of temperature regulation.
How homoeothermic animals can retain heat?
Homoeothermic animals can retain heat in a variety of ways when
the environment is cold (to conserve the body heat).
They use their fur, fat and feathers.
For example, the arctic fox uses its fluffy tail as extra insulation
when it curls up to sleep in cold weather.
Homeothermic animals also use vasoconstriction in response to the
coldest environment.
Vasoconstriction: is the narrowing of blood vessels to the skin by
the contraction of their smooth muscles to reduce blood flow in the
peripheral blood vessels and retain heat.
Shivering: is another way of maintaining body temperature in cold.
Shivering is caused by involuntary contractions of your muscles.
Muscle contractions require energy from respiration that releases
heat to warm the body.
Figure: Temperature regulation during cold weather by puffing up feathers in birds (left),
raising hair in human (middle) and fur in fox (right)
As animals grow in size, their inside volume increases and the outside
surface area decreases. This affects the surface-area-to-volume ratio
or the surface-to-volume ratio of animals, which consequently affects
heat loss.
The greater the surface area-to-volume ratio an animal has, the
more heat loss it will have, and the smaller the surface area- to-
volume ratio an animal has the less heat loss it will have.
The smaller the animal, the higher the surface area-to-volume ratio
it will have, so it will have the higher heat loss.
Example 1: Since the size of an elephant is high, the surface area to
volume ratio becomes smaller than the surface area to volume ratio of
a rabbit.
Example 2: On the other hand, the larger the animal, the smaller the
surface area-to-volume ratio it will have.
The ratio of metabolism to SA
One way to become more efficient is to divide; another way
is to develop organelles that perform specific tasks. Eg
eukaryotic cells.
Substrate: The molecule the enzyme works on (acts on) is called the substrate, and their
shapes must match.
Functional sites in the enzymes system:
A. An active site/Catalytic site:
is a region on the surface of an enzyme to which substrates will bind and catalyses a chemical
reaction.
It is the region on the enzyme surface that catalyzes the chemical reaction, in other words, it is the site(s)
which manipulates the substrate to help rapidity of the chemical reaction. It may be separated from the
substrate-binding site by a large or a small distant or they may be combined into one site.
B. Substrate-binding site
Substrate-binding site at which substrate specifically binds and the active site is the site that carries out the
chemical action.
C. Allosteric site
The term allosteric site means “the other site” and allostery means “a change in shape”. This indicates that
when an allosteric effector non-covalently binds at allosteric site (a site other than active and substrate
binding site), it causes a conformational change in the enzyme particularity at the active site(s) that
decreases or increases the enzyme activity.
3.2 Properties and functions of enzymes
3.2.1 General properties of an enzyme
•The general properties of enzymes are:
Enzymes accelerate the reaction rates.
Enzymes are highly specific in their action
They neither affect the nature of products formed
They remain chemically unchanged during the reaction
The enzyme is not used up and available to catalyse further reactions
A. The physical properties of enzymes
•The physical properties of enzymes include denaturation, solubility, colloids,
biocatalysts, precipitation, molecular weight, and enzyme activity.
•Denaturation: is the process of breaking the intra and inter-molecular non-
covalent bonds that distort the shape and active site of the enzymes.
• Enzymes are denatured by high heat (above 40ºC), alternation in the pH (too
low or too high), heavy metals and high salt concentrations, solvents and
other reagents.
•Solubility is the property of enzymes that allow them to be dissolved in water,
salt (NaCl), diluted glycerol and alcohol causing denaturation.
Cont…
• colloidal nature The colloidal nature of enzyme is the tendency of having little or
no dialysis cross the semipermeable membrane due to the large size or high
molecular weight. (Property between solution and suspension)
• The biocatalyst property is the activity of enzymes in which very small quantities
or a small amount of enzyme is enough to convert a large quantity of substrate and
remain unchanged after the reaction.
• Or small amount, of enzyme can affect a large amount of substrate
• Enzyme precipitation is the separation of enzymes for analysis using different
aqueous or ethanol solvents.
• Molecular weights of enzymes are large protein biomolecules that hold
polypeptide chains of various amino acid sequences in enzymes having a high
molecular weight.
• Enzymatic activity is the general catalytic properties of an enzyme.
• It depends on factors such as temperature, pH, and enzyme concentration and
substrate concentration.
• Enzymes show the highest activity at optimum temperature and pH that a low
concentration of enzymes and substrates slows down the enzymatic reaction.
Physical properties of Enzymes
B. Chemical properties of enzymes
• Enzyme chemical properties are sensitivity, regulations, specificity,
catalysis and reversibility reactions.
• Heat and PH Sensitivity:
• Enzymes are sensitive to Heat (temperatures) and PH (acidity and
basicity). They work best at optimum levels.
• Regulation: is the process of controlling the activity of enzymes by
activator and inhibitor molecules.
• Catalysis: is the process of the acceleration of a chemical reaction by
a catalyst. Enzymes are biological catalysts that possess high catalytic
efficiency.
• They can transform about 100-10,000 substrates per second.
• The reactions catalyzed by the enzymes show a 103-108 times faster
reaction rate in comparison to the non-catalyzed reactions.
• Reversibility: is the ability of enzymatic biomolecules to catalyze
various metabolic (anabolic and catabolic) reactions.
• Enzymes can catalyze biochemical reactions in both forward and
reverse directions.
Enzyme specificity
• Specificity means: The quality of being specific rather than
general
• Enzyme specificity is a property of the enzyme that
describes how restrictive the enzyme is in its choice of
substrate.
Types of specificity of enzymes
• Bond specificity is a relative specificity of enzymes, which
indicates that enzymes are specific for a bond.
• Group specificity is a structural specificity of enzymes, which
describes that enzymes are specific for a group.
• Substrate specificity is the feature of enzymatic activity where
a particular substrate.
• A completely specific enzyme would have only one substrate.
• Absolute/compelete specificity - the enzyme will catalyze only
one reaction.
• Optical specificity is when enzymes act on the substrate optical
configuration.
• Co-factor specificity is the enzymatic specificity to the
substrate and co-factors.
• Linkage specificity - the enzyme will act on a particular type
of chemical bond regardless of the rest of the molecular
structure.
Figure : Chemical properties of enzymes
.
Functions of enzymes in the human body
• Enzymes help speed up chemical reactions in the human body.
• Each cell in the human body contains thousands of enzymes that
provide help in facilitating chemical reactions within each cell.
• They are essential for respiration, digesting food, the liver, muscle,
and nerve function.
• Enzymes are also used as markers of the states of various diseases like
-myocardial infraction (The middle muscular layer of the heart wall)
-jaundice (symptom of gallstones or liver infection or anemia),
-pancreatitis (Inflammation of the pancreas)
-cancer and neurodegenerative disorders etc.
• Examples of enzymes convert macromolecules into their monomers
Sucrase breaks down a sugar called sucrose.
Lactase breaks down lactose, a kind of sugar found in milk products.
Carbohydrase breaks down carbohydrates into sugars.
Lipase breaks down fats into fatty acids.
Protease breaks down protein into amino acids
Table: Some of enzymes in the body and their functions
Enzyme Function
Lipases Split fats found in the blood, gastric juices, pancreatic
secretions, intestinal juices, adipose (fatty) tissues and
participate in digestions.
Amylase Amylase exists in saliva and helps in changing starches
into sugars.
Maltase Maltase exists in foods such as potatoes, pasta and beer
and saliva breaks the sugar maltose into glucose.
Trypsin Found in the small intestine, breaks proteins down into
amino acids.
Lactase Found in the small intestine, breaks lactose, the sugar in
milk, into glucose and galactose.
Helicase Unwinds DNA
DNA Polymerase An enzyme responsible for forming new copies of DNA
in
the form of nucleic acids molecules
Breaks down the neurotransmitter acetylcholine in
Acetyl nerves and muscles
cholinesterase
3.2.2 The function of enzymes
How do enzymes act as catalysts?
Enzymes perform their function by lowering a reaction's activation energy.
Activation energy: is the energy required to start a reaction.
The lower the activation energy, the faster a reaction happens.
The rate of a chemical reaction: is the rate at which reactants are converted into
products.
Therefore, enzymes increases turnover rate of the reaction.
Turnover rate: is the number of molecules of reactants that form enzyme-substrate
complexes with each molecules of an enzyme per second.
The turn over number of molecules is the number of substrates converted by one
enzyme molecule per second at saturated (fully occupied) active sites.
Before forming the results, the reactant must „climb an activation energy hill‟
before anything happens.
Under normal conditions, very few molecules have sufficient kinetic energy to
„climb the activation energy hill‟, so the reaction proceeds slowly.
More reactant molecules can meet this lower energy requirement and so the
reaction proceeds more quickly
Each enzyme has an active site with a unique shape that speeds up metabolism or
chemical reactions in our bodies and builds substances in all living things.
Enzymatic catalysis relies on the action of amino acid side chains arrayed in the
active center.
Activation energy for catalyzed and unanalyzed reactions
.
3.3 Protein structures
• Protein structure is a polymer of aminoacids joined by peptide bonds with three-dimensional
arrangements of atoms in amino acid chain molecules.
• Proteins have different structures.
• The protein complex macromolecules have four structural levels:
1. Primary structure 2. Secondary structure
3. Tertiary structure 4. Quaternary structure
1. The primary structure of proteins
• The primary structure of proteins makes up amino acid sequences based on the side-chain
substituents that differ by the chemical, physical, and structural properties.
• It is the sequence of amino acids linked together to form a polypeptide chain through peptide
bonds created during the protein biosynthesis process.
Two amino-acids bond to form a dipeptide and water, during a condensation reaction. The
covalent bond between them is called a peptide bond.
Proteins with fewer than 50 sequences are peptides, and proteins with longer than 50
sequences of amino acids are polypeptides.
• Humans require 20 amino acids out of which 10 amino acids are synthesized in the human
body, and the rest 10 amino acids are obtained from diets.
• Cells use 20 different standards of L-α-amino acids containing basic amino acids and acidic
• carboxyl groups for protein construction.
2. The secondary structure of proteins
• The secondary structure of a protein is a folded structure formed within a
polypeptide due to interactions between atoms of the backbone based on hydrogen
bonding and containing α-helix
• and ß-sheet types of strands.
The α – Helix
• α-helix – protein turns like a spiral – fibrous proteins (hair, nails, horns)
• The α-helix is a right-handed coiled
strand and the side-chain substituents
of amino acid groups extend to the
outside and form hydrogen bonds
with oxygen (C=O) in the strand with
the hydrogen of each (N-H) group of four amino acids to make the structure stable.
• ß-pleated sheet: ß-sheet – protein folds back on itself as in a ribbon –globular
protein
3. The tertiary structure of proteins
• The tertiary protein structure is the three- dimensional shape of protein molecules
that bend and twist to achieve the maximum stability or the lowest energy state.
• The tertiary structure of protein is referred to as a specific mode of spatial
arrangement of the polypeptide chain. It is the structure of an enzyme.
• It is fashioned by many stabilizing forces due to the bonding interactions between the
side-chain groups of amino acids.
30 structure is determined by interactions between R groups, rather than interactions
between backbone constituents.
These interactions between R groups include
hydrogen bonds:between –OH, –NH2,,
ionic bonds:
hydrophobic interactions,
disulphide bonds/bridges : Covalent bonds &
van der Waals interactions.
4. The quaternary structure of proteins
• Quaternary structure results when two or more polypeptide (multiple folded protein)
chains form one macromolecule
• It is the association of several protein chains or subunits into closely packed
arrangements with their own primary, secondary, or tertiary structures and held
together by the hydrogen bonds.
• Collagen is a fibrous protein consisting of three polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting of four polypeptides: two alpha and
two beta chains
Fig b. Hemoglobin
3.4 Enzyme substrate models
• Enzyme substrate models describing that the shapes of the active site and the
substrate complement to fit into the binding active site perfectly.
• The models suggest that the enzyme catalyzes the reaction by lowering the
activation energy. However, they differ in explaining how the substrate binds
to the active site of the enzyme
• There are two different of enzyme-substrate binding models that we will
look at in this section:
i. the lock and key model and
ii. the induced fit model.
1. Enzyme lock and key model
• Proposed in 1894 by a German biochemist named Fischer.
• The model proposes that the shapes of the substrate molecules are
complementary to that of the active site, rather like the shape of a key is
complementary to that of the lock it fits.
• States fit between the substrate and the active site of the enzyme is exact.l
• The substrat and enzyme fit exact like a key fits into a lock very precisely
• The model explains enzyme specificity
• This explains the loss of activity when enzymes denature.
92
The Induced Fit Hypothesis
Proposed in 1958 by Koshland.
This model suggests that the active site and the substrate
aren‟t naturally complementary in shape, but the binding of substrate
molecules produces a conformational change in the active site.
Substrate + enzyme, induces a change in the enzyme‟s conformation
This allows the substrate and active site to bind fully.
The conformational change also puts the substrate molecules under
tension, so they enter a „transition state‟ and are able to react because
of the lowered activation energy.
Most biologists now prefer the induced-fit model over the lock and-
key model:
As it explains other properties of enzymes, such as enzyme inhibition,
The rate of a chemical reaction is the rate at which reactants are converted into products.
Some proteins can change their shape (conformation) Active site
moulded to a precise conformation.
The bonds of the substrate are stretched to make reaction easier
93
(lowers activation energy).
3.4.2 Enzymatic transition state
The transition state is: is the intermediary state of the reaction, when the
molecule is neither a substrate or product or product.
An enzymatic transition state is the reaction rates of elementary chemical
reactions and assumes chemical equilibrium between reactants and
activated transitions.
Transition-state stabilization: The active site often acts as a flexible
molecular template that binds the substrate in a geometric structure
resembling the activated transition state of the molecule (see T* at the top
of the curve ).
By stabilizing the substrate in its transition state, the enzyme greatly
increases the concentration of the reactive intermediate that can be
converted to product and, thus, accelerates the reaction.
Where: E = Enzyme
S = Substrate, ES = Enzyme substrate
combined, ES*= Enzyme substrate
complexes , EP= Enzyme product,
E + S ES ES* EP E + P
94
3.5 Enzyme regulation
• Enzyme regulation is a control system for enzymatic activities.
• Enzyme regulation refers to the multiple mechanisms available to
control the activity of the enzymes.
• The enzymes are turned “on” or“off” depending on the organisms
need.
• It is adapting enzymatic activities by other molecules or metabolic
cells to either increase or decrease the activities.
• A regulatory enzyme is the one in a biochemical pathway through
which it responds to the presence of certain other biomolecules
and regulates the pathway activity.
• It requires an extra activation process to pass through some
modifications and functions.
• Types of enzyme regulation
i. Allosteric enzymes regulation
ii. Genetic and covalently modulated enzymes
iii. Enzyme inhibition
95
1.Allosteric enzymes
Allosteric enzymes: are enzymes that have additional binding sites other than
the active site or substrate binding site.
Allosteric regulation occurs when an activator or inhibitor molecule binds at
specific regulatory site on the enzyme.
The binding molecule is called an effector, it cab be inhibitor as well as
activator.
The binding of the effector molecule/Allosteric regulatory cause/induces
conformational changes of the enzyme, leading to changes of catalytic
properties or reduce enzyme activity.
Effectors lead to conformational changes in a concrete part of the enzyme that
affect the overall conformation of the active site, causing modifications in the
activity of the reaction
Activator increases the activity of an enzyme, whereas inhibitor decrease the
activity after binding.
Allosteric enzymes contain two binding sites:
i. Active site/catalytic site and
ii. Allosteric site/regulatory site
for binding effectors and
substrates respectively.
96
Cont…
Thus, allosteric effector is called negative allosteric effector (or feedback inhibitor)
when the resulting conformational change decreases the enzyme activity. However,
the allosteric effector is called positive allosteric effector (or feedback activator) if the
resulting conformational change increases the enzyme activity.
+Allosteric +
inhibitor Conformational substrate Substrate binding
Allosteric enzyme Change site unfit
+Allosteric + +
activator Conformational substrate Perfect binding Products
Allosteric enzyme
Change
97
2. Genetic and covalent modification
Genetic regulation is one of the many mechanisms in which the structure of
the enzyme can be modified further by adding additional special group to
specific location.
The genetic and covalent modification modifies the protein surface and
facilitates intracellular delivery.
Genetic modification of enzymes is to improve the properties of enzymes
and gain active and inactive forms.
Covalent modulated enzymes are active and inactive forms of the enzymes
altered due to covalent modification of structures catalyzed by other
enzymes.
Covalent modifications are enzyme-catalyzed alterations of synthesized
proteins by the addition or removal of chemical groups.
Modifications can target a single type of amino acid or multiple amino acids
and will change the chemical properties of the site.
Enzyme regulation occurs by the addition or elimination
of some molecules attaching to the enzyme protein.
Examples: Phosphorylation: is the addition of
phosphate groups to proteins. It is the most frequent
regulatory modification mechanism in our cells
3. Enzyme inhibition
Enzyme inhibition: is a decrease in enzyme activity by enzyme
inhibitors.
Enzyme inhibitors are molecule that binds to an enzyme and blocks
its activity. They decreases the efficacy of the enzyme
There are two types of inhibitors.
i. Reversible inhibitors and
ii. irreversible inhibitors
Reversible inhibitor:
The reversible inhibitor binds the enzyme non-covalently.
So they can easily reversed.
Reversible inhibitors can be competitive and uncompetitive.
Irreversible inhibitors
It is a substance that permanently blocks the action of an enzyme. 99
1. Competitive inhibitor
The inhibitor has a structural similarity to the substrate.
They compete with the substrate for the active site of the enzyme
So, it binds the active site (substrate-binding site) of in competition
with the substrate depending on their relative concentration.
Therefore, increasing substrate concentration or lowering inhibitor
concentration reverses enzyme inhibition.
Competitive inhibitor is a molecule that blocks the binding of the
substrate to the active site.
• Enzyme can only bind to either substrate or inhibitor at a time.
102
3.6 Types of enzymes
Enzymes can be classified into various types.
Enzyme types are based on how enzymes that bind specific molecules together to
form new molecules and enzymes that break specific molecules apart into separate
molecules.
Enzymes possess three types of names. They are:
•classical (trivial) or common(recommended)
•Enzyme structural classification
•systematic( scientific) names or basic classification
Trivial name
Trivial names were coined on the basis of the source from which an enzyme
was extracted eg. Pancreatic lipase,or for Greek/Latin name of the process
(eg. Pepsin - to digest, trypsin-to wear down).Consequently it may not be
possible to figure out the reaction from a trivial name.
Recommended name
Most commonly used enzyme names have the suffix "-ase" attached to the
substrate of the reaction (for example, glucosidase,urease, sucrase), or to a
description of the action performed (for example, lactate dehydrogenase and
adenylyl cyclase).
3.6.1 Enzyme structural classification
Deals with the separation of an enzyme into simple proteins (active)
and conjugated proteins (holoenzymes).
There are two types of enzymes
i. Simple (only protein) ii. Complex or holoenzymes or conjugated proteins
The conjugated protein is divided into two:
i. Apoenzyme (protein part): Are inactive groups
ii. cofactor (non-protein part): Are inactive groups
Cofactor (non-protein part) can be divided into two:
i. Prosthetic groups:
usually small inorganic molecule or atom;
usually tightly bound to apoenzyme
ii. Coenzyme
large organic molecule (Vitamins)
loosely bound to apoenzyme
3.6.2 Basic or systematic classification of enzymes
Enzymes are composed of six classes based on what and how they react, the types
of reactions they catalyzed, and the end suffix “ase”.
The International Union of Biochemistry and Molecular Biology (IUBMB) have subdivided
enzymes into classes, subclasses and sub-subclasses and give every enzyme a written name
and a code digital name.
The written name is formed of the substrate name, the coenzyme name and name of the
chemical process.
The digital name is of four digits, the first refers to the enzyme class, the second refers to the
subclass, the third refers to the sub-subclass and the fourth refers to the name of the
individual enzyme itself.
In addition to its name an enzyme is also given a unique identification
number (ID-number). An enzyme's identification number is known as
enzyme code (E.C) or enzyme commission number.
Its Enzyme Commission number (E.C. 2.7.1.1.)
(2) denotes the class name (transferase);
(7) denotes the subclass (phosphotransferase);
(1) denotes a subsubclass phosphotransferase with a hydroxyl group as acceptor;
(1) denotes D -glucose as the phosphoryl group acceptor.
For many enzymes, a trivial name is more commonly used—in this case hexokinase.
According to this system there are 6 classes of enzymes.
The six classes of enzymes
1. Oxidoreductases: Are a class of enzyme that catalyzes oxido-
reduction reactions.
E.g. oxidases, oxygenases, reductases, dehydrogenases & peroxidases.
It catalyzes the transfer of electrons from one molecule (oxidant) to
other molecule (reductant) reactions in the following pattern:
A- + B ⇌ A + B- , where A is the oxidant and B is the reductant.
2. Transferase: Are enzymes catalyzing the transfer of a chemical group
from one compound to the other.
They transfers functional groups like methyl from one donor
molecule to acceptor molecule. A-B + C ⇌ A + B-C
E.g: aminotransferases, glycosyltransferases, methyltransferases,
acyltransferases, phosphotransferases (kinases)
3.Hydrolases: These are enzymes catalyzing the process of hydrolysis (breakdown of
the compound by addition of water), e.g., thiolases, amidases, ribonucleases,
deoxyribonucleases, hydrolytic deaminases, phospholipases, phosphatases,
glycosidases, esterase and peptidases. A-B + H2O ⇌ A-H + B-OH
Cont…
4.Lyases: these are enzymes, which catalyze breakdown of substrates by mechanisms
other than hydrolysis and oxidation.
They are enzymes that cleave bonds by other means rather than hydrolysis or
are enzymes that cleave bonds by other means rather than hydrolysis or oxidation in
which two or more substrates are involved in one reaction. A-B ⇌ A = B + X-Y
5.Isomerases: these are enzymes catalyzing isomerization, e.g.,
Epimerases, e.g., UDP-Glucose UDP-Galactose.
Cis-trans-isomerase, e.g., trans-Retinol cis-Retinol.
Mutase, e.g., glucose-6-phosphate glucose-phosphate.
Aldo-keto-isomerase, Glucose-6- phosphate Fructose-6- phosphate.
X Y Y X
A-B ⇌ A- B
6.Ligases or synthetases:
-These are enzymes catalyzing the process of ligation or binding of 2 molecules together
in the presence of ATP (synthetase),
- are enzymes that catalyze the joining of two molecules with concomitant hydrolysis of
the di-phosphate bond in ATP
e.g., Fatty acid + CoASH + ATP Acyl-CoA + AMP + PPi.
Carboxylases are ligases.
A +B ⇌ A-B
Cont…
Its Enzyme Commission number (E.C. 2.7.1.1.)
For many enzymes, a trivial name is more commonly used—in this case
hexokinase.
According to this system there are 6 classes of enzymes.
Systematic name
The International Union of Biochemistry and Molecular Biology (IUBMB) have
subdivided enzymes into classes, subclasses and sub-subclasses and give every
enzyme a written name and a code digital name.
The written name is formed of the substrate name, the coenzyme name and
name of the chemical process.
The digital name is of four digits, the first refers to the enzyme class, the
second refers to the subclass, the third refers to the sub-subclass and the fourth
refers to the name of the individual enzyme itself.
Example:The systematic name of the enzyme which catalyzes:
For many enzymes, a trivial name is more commonly used—in this case
hexokinase.
According to this system there are 6 classes of enzymes.
The six of Enzymes
6.Ligases or synthetases:
-These are enzymes catalyzing the process of ligation or binding of 2
molecules together in the presence of ATP (synthetase),
e.g., Fatty acid + CoASH + ATP Acyl-CoA + AMP + PPi.
Carboxylases are ligases.
A +B ⇌ A-B
Structure of enzymes
Enzymes
113
Many enzymes require the presence of other compounds - cofactors -
before their catalytic activity can be exerted.
Coenzyme classification
(1) Metabolite coenzymes - synthesized from
common metabolites
(2) Vitamin-derived coenzymes - derivatives of
vitamins
Vitamins cannot be synthesized by mammals, but
must be obtained as nutrients 115
Vitamin-Derived Coenzymes
116
NAD+ and NADP+
• Nicotinic acid (niacin) an nicotinamide are precursor of
NAD and NADP
• Lack of niacin causes the disease pellagra
NAD and
NADP are
coenzymes
for
dehydro-
genases
117
FAD and FMN
• Flavin adenine dinucleotide (FAD) and Flavin
mononucleotide (FMN) are derived from riboflavin (Vit B2)
• Flavin coenzymes are involved in oxidation-reduction
reactions
118
3.7 Factors affecting enzyme action
Enzymes work best within specific temperature and pH ranges and at optimal
conditions.
optimal conditions: is the condition under which particular enzyme is most active and
effective.
There are varieties of factors that affect the activity of enzymes: these are
temperature, pH. inhibitors,
activators, radiation, water,
changes in enzyme concentration,
substrate concentration,
changes in enzyme and
and end-product concentrations.
Temperature
All the enzymes work best within the
specific ranges of optimum temperatures,
Low or high temperature
causes an enzyme to lose its activity
and ability to bind a substrate and denatured.
Once enzymes denatured,
they cannot be renatured.
PH
PH: enzymes function at optimum pH (the potential of hydrogen ions) that ranges
from too low (strong acid) to too high (too alkaline) pH.
Substrate concentration
Substrate concentrations: enzymes require a maximum limit of substrate
concentration to bind.
at a low substrate concentration there are many active sites that are not
occupied. This means that the reaction rate is low.
When more substrate molecules are added, more enzyme-substrate
complexes can be formed.
As there are more active sites, and the rate of reaction increases.
Eventually, increasing the substrate concentration yet further will have no
effect.
The active sites will be saturated so no more enzyme-substrate complexes
can be formed.
• 1.Radiation: damages enzyme activities by reducing in
enzymatic efficiency and creating disorders in the
macromolecules.
• 2. Water: affects the performance of enzymes’ activity beyond
its optimum level.
3. End product (Feedback) inhibition
• is a cellular control mechanism in that the end product inhibit
enzyme's activity. In feedback inhibition, the endproduct binds
to the
• allosteric site of the enzyme and change the structure of the
active site. This prevents the
• enzyme to perform its activity. Due to feedback inhibition, a
cell is able to know whether the amount of a product is
enough for its subsistence or not
• Example: The drug Tipranivir used to treat HIV blocks the
activity of a viral genome enzyme to make more copies as a
reversible inhibitor.
I.Effect of Enzyme Concentration
When every other variable remains constant the rate of a reaction
increases linearly as concentration of an enzyme increases
3.9 Application of enzymes in industries and their benefits
• Application of enzymes is the use of enzymatic biochemical reactions for chemical conversion
process that are driving forces of great change for productivity of various industries.
• Enzyme protein catalytic activity is efficient enough (100s to 1000s) of times higher than that
of inorganic catalyst
3.9.1 Uses of enzyme application
• The application of enzymes are widely used in food, feed, textile, papermaking, leather and
detergents, pharmaceutical and other industrial productions.
• Examples:
1. Enzymes break down larger complex molecules into simpler molecules in our body where they
can be used to fuel our digestive systems and cellular respirations.
2.Most enzymes used for food industry were extracted from the internal organs of animals and
plants, but now most enzymes are obtained by microbial fermentation.
3.Enzymes cause billions of chemical reactions to happen at lightning speed inside the cells of
our body.
4.Enzymes improve the utilization of feed rate of starch, protein, and minerals and degrade the
anti-nutritional factors in animal feed, prevent animal indigestion and improve feed
digestibility.
5.In the pharmaceutical industry, enzymes are used in drugs, antibiotics, household products to
speed up chemical reactions and synthesis.
6. Enzymes are powerful tools in sustaining a clean environment in several ways.
7.Washing powders are enzymes used to break down protein, starch and fat stains on clothes
Table: he applications and functions of enzymes
.
3.10 Malting in Ethiopian tradition
• Malting (sprouting) is a widely applied traditional technology.
• It is the process of steeping, germinating and drying grain to convert
it into malt.
• Malting is the limited controlled germination of grains in moist air,
which results in the mobilization of amylases, proteases and other
enzymes that hydrolyze and modify the grain components and its
structure.
3.10.1 Steps of modern malting
• There are three steps to modern malting, steeping, germinating and
kilning, and these will be discussed in this section