ADVANCE BIOLOGY: QUARTER 3

Cell metabolism
 Metabolism – all biochemical reactions within the
body.
 Basal Metabolic rate – energy requirement of an
awake person at rest
– energy needed at a person’s lowest level
of cellular function
– Basal Metabolic Rate (BMR) of an
average man is around 7,100 kJ/day
– BMR of average woman is around
5,900 kJ/day
 Nutrients – any ingested chemical that is used for Chemical Reactions
growth, repair, and maintenance of the body
 Catabolism – breakdown of complex structures  Chemical reactions either release or store energy.
into simpler forms  A living organism produces thousands of
 Anabolism – process by which simpler molecules endergonic and exergonic chemical reactions.
combine to build more complex structures - All of these combined is called
metabolism.
Law Of Thermodynamics and How - A metabolic pathway is a series of
chemical reactions that either break down
They Apply to Living Organisms a complex molecule or build up a complex
molecule.
FIRST LAW OF THERMODYNAMICS
EXERGONIC REACTIONS
 Also known as the Law of Conservation of
Energy.  These reactions release the energy in covalent
 Energy cannot be created nor destroyed but it can bonds of the reactants.
be transferred from one form to another.  ATP to ADP
 An organism cannot create the energy that it
requires to live. Example:
- Plants - Cellular respiration
- Sponge - Digestion
- Bacteria
- Humans ENDERGONIC REACTIONS
Examples:
 Light energy to chemical energy (from sun to  Requires an input of energy; products contain more
sugar in a plant) chemical/potential energy.
 Water behind a dam (potential energy) is  ADP to ATP
released (kinetic)
Example:
SECOND LAW OF THERMODYNAMICS - Photosynthesis

 States that energy transformations increase disorder ENERGY COUPLING

or “entropy”.
 Some energy lost as heat that the organism uses
anyway.
 Living systems have adapted to transfer energy
efficiently.
 Energy cannot be changed from one form to
another without a loss of usable energy.
Biological systems follow the laws of thermodynamics,
and to offset entropy, energy input must exceed energy lost
from and used by an organism to maintain order. Energy
flows through living things, it does not cycle.
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 Energy released from exergonic reactions drive
endergonic reactions.
ENZYMES
 Chemical reactions can be enzymatic.
 Enzymes are also called catalysts. They speed up
the rate of chemical reactions by reducing
activation energy.
 Enzyme – helper protein molecule
 Substrate – molecule that enzymes work on
 Products – what the enzyme helps produce from
the reaction
 Active Site – part of enzyme that the substrate
molecule fits into
- Lock and Key
 Activation Energy – energy needed to start a
chemical reaction
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 ADVANCE BIOLOGY: QUARTER 3
Cell metabolism

 Activation energy for the acid catalyzed hydrolysis

of sucrose is 6.66 KJ mol while the activation
energy is only 2.15 KJ mol when hydrolysis is
catalyzed by the enzyme sucrase.

EXAMPLES OF ENZYMES
SUBSTRATE LOCATION IN
ENZYMES
(REACTANT) BODY
Amylase Carbohydrates/Sugars Mouth
Various
Lipase Fats
locations
Pepsin Proteins Stomach
Trypsin Proteins Small Intestine INDUCED FIT THEORY
Lactase Dairy Small Intestine  Induced Fit Analogy was first postulated by Daniel
Koshland.
ENZYME SPECIFICITY  Involves the changing of the conformation of the
active site to fit the substrate after binding.
 In a chemical reaction, a specific type of enzyme  There are amino acids that aid the correct substrate
can act on a specific type of substrate only. to bind to the active site which leads to shaping of
 1 enzyme per type of substrate. the active site to the complementary shape.
Example: Enzyme amylase for carbohydrates,
pepsin for proteins, lipase for lipids.

HOW ENZYMES WORK

SUBSTRATE
ENZYMES PRODUCTS
(REACTANT)
Hydrogen peroxide Oxygen gas + water
Catalase
(H2O2) (O2 + H2O)
Mechanism of enzyme activity Diastase Starch Maltose
Simple sugars
LOCK AND KEY THEORY Pectin (in plant cell
Pectinase (releases juices from
walls)
cells)
 Lock and Key analogy first postulated in 1894 by
Pepsin Proteins Short polypeptides
Emil Fischer.
 In this analogy, the lock is the enzyme and the key Soluble casein (milk Insoluble casein
Rennin
is the substrate. Only the correctly sized key protein) (curdled milk)
(substrate) fits into the key hole (active site) of
the lock (enzyme).
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 ADVANCE BIOLOGY: QUARTER 3
Cell metabolism
REGULATION OF ENZYME
ACTIVITY
COENZYMES
 Coenzymes = organic (non-protein) molecule
required for proper functioning of enzyme
 e.g. NAD+, FAD+, vitamin complexes
 Coenzymes often remove electrons from the
substrate and pass them to other molecules

COFACTORS
 Cofactors = inorganic molecule required by
enzyme for proper functioning of enzyme
 e.g. copper (Cu+), zine (Zn++), iron (Fe++),
SUBSTRATE CONCENTRATION
magnesium (Mg++), potassium (K+), and calcium  Reaction rate increases with increasing substrate
(Ca++) ions concentration.
 The cofactors bind to the enzyme and participate in  There is a limit to this increase however – once all
the reaction by removing elections, protons, or active sites are occupied (saturated), adding more
chemical groups from the substrate.
substrate will not increase the reaction rate.
THE COENZYME PREPARES THE
ACTIVE SITE FOR CATALYTIC ACTIVITY

ENZYME CONCENTRATION

FACTORS THAT AFFECT ENZYME  As the enzyme concentration increases the rate of
the reaction increases linearly, because there are
ACTIVITY more enzyme molecules available to catalyze the
reaction. At very high enzyme concentration the
TEMPERATURE substrate concentration may become rate-limiting,
so the rate stops increasing. Normally enzymes are
 Each type of enzyme has a temperature range at present in cells in rather low concentrations.
which it works best.
- Human enzymes work best at 30-40°C
- Hot springs bacteria at 85°C
- Antarctic ice fish at 2°C
 Enzyme activity increases as the environment
reaches that ideal temperature.
 Activity slows outside of that range.

PH
 Enzymes have a specific pH range at which they
will work. ACTIVATORS
 At an extreme temperature or pH, an enzyme can
denature (change shape and become ineffective)  Some chemicals increase the activity of enzyme
and they are called activators.
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 ADVANCE BIOLOGY: QUARTER 3
Cell metabolism

INHIBITORS
 Inhibitors – chemical that interferes with an
enzyme’s activity.
 Competitive Inhibitors
– Block substrates from entering the active
site
– Reduce an enzyme’s productivity
 Noncompetitive Inhibitors
– Bind to the enzyme somewhere other
than the active site, change the shape of
the active site, prevent the substrate from
binding.

EXAMPLES OF ENZYME INHIBITORS

 Poisons
– Inhibits an enzyme required for normal
function of the insect nervous system
Example: Malathion

 Antibiotics
– Inhibits an enzyme bacteria use to make
cell walls
Example: Penicillin

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