Enzymes

1) Catalyst = a substance that increases the rate of

a chemical reaction without itself undergoing any
permanent chemical change.
a) Increase the rate of a reaction
b) Never change by the reaction (so can be used
again and again)
c) Do not change the nature of the reaction--the
reaction could have occurred without the enzyme, just
much slower
d) Lowers the activation energy of the reaction
1. Mechanism of Enzyme Action
1. Conformation: is the special shape for each enzyme
2. Active Site: Is the particular place within the enzyme where
the catalyst take place
3. Substrates: Are the molecules that use the enzyme to be
converted in other different product
4. Lock & Key model: The specific shape of the substrates,
FIT perfect into the active sites of that particular enzyme
5. Induce Fit Model: That fit may not be perfect at first,
however the substrate may adjust its shape to the active site
6. Product: The enzyme/substrate complex produce a
totally new molecule/s without altering the Enzyme
structure
Mechanisms of Enzyme Activity, cont

5. When a substrate binds to the active site of an

enzyme, it forms temporary bonds, weakening the
original bonds of the substrate and allowing them to
break easily.
Naming Enzymes

1. The first enzymes discovered were given arbitrary

names. An international committee later decided to end
all enzymes with the suffix –ase.
2. They also decided to make the first part of the name
apply to the function of the enzyme.
a. Phosphatases remove phosphate groups.
b. Synthetases and synthases catalyze dehydration
synthesis.
c. Hydrolases – promote hydrolysis
d. Dehydrogenases – remove hydrogen atoms
e. Kinases – add phosphate groups
f. Isomerases – rearrange the atoms
Isoenzymes

a. Because names are given to enzymes based on

function, an enzyme that does the same job in two
different organs has the same name.
b. However, the molecules may be slightly different
(in areas outside the active site) and are called
isoenzymes; useful for detecting and diagnosing
certain diseases
Control of Enzyme Activity

1. Measured by the rate at which substrate is

converted to product
2. Influenced by:
a. Temperature
b. pH
c. Concentration of cofactors and coenzymes
d. Concentration of enzyme and substrate
e. Possible stimulatory or inhibitory effects of
products on enzyme function
 Effects of Temperature

1. An increase in
temperature will
increase the rate
of reactions until
the temperature
reaches a few
degrees above
body temperature.
2. At this point, the
enzyme is
denatured.
 Effects of location on optimum pH

Enzymes exhibit peak activity

within a narrow pH range
called the pH optimum.
pH changes will result in
enzyme conformational
changes
Optimum pH reflects the pH
of the fluid the enzyme is
found in
a. Stomach vs. saliva
vs. small intestine
Coenzymes

1. Most enzymes need additional small molecules to

aid in a reaction.
2. Coenzymes are organic molecules derived
from water-soluble vitamins.
3. They transport hydrogen atoms and other small
molecules between enzymes.
Cofactors

1. Cofactors help
form the active site
through a
conformational
change of the
enzyme or help in
enzyme-substrate
binding.
2. Cofactors are
metal ions such as,
Ca2+, Mg2+, Mn2+,
Cu2+, Zn2+
Enzyme Activation

1. Enzymes, particularly of the digestive system,e

often produced in an inactive form called a
zymogen (inactive enzyme) that is activated when
needed
a. Example: pepsinogen 🡪 pepsin
2. It often requires additional enzymes to
phosphorylate or dephosphorylate the molecule.
3. Enzyme inhibition can be controlled through
turnover, by which enzymes are degraded.
Substrate Concentrations
1. As the substrate
concentration
increases, so will the
rate of the reaction until
the enzyme becomes
saturated
2. Saturated means that
every enzyme in the
solution is being
used.
3. Adding more substrate
will not increase the
rate of the reaction
Reversible Reactions

1. Sometimes a single enzyme can drive a reaction in

two directions, depending on the concentration of
substrate/product.
2. When one side gets higher, the other reaction
reverses.
3. This is called the law of mass action.
4. Example: the enzyme carbonic anhydrase (CA)
at the systemic capillaries
H2O + CO2 ↔ H2CO3
Metabolic Pathways/Linear pathway

1. Most reactions are linked together in a chain (or

web) called a metabolic pathway.
2. These begin with an initial substrate and end with
a final product, with many enzymatic steps along
the way. The linear pathway is not common.
Branched Metabolic Pathways
a. Most include branches where several products can be
produced.
End Product Inhibition

a. Branch points are often inhibited by a form of

negative feedback in which one of the final
products inhibits the branch point enzyme.
b. In the process called allosteric inhibition, the
product binds to the enzyme at a location away
from the active site and changes the 3D
conformation of the enzyme.
c. Prevents the final product from accumulating
End Product Inhibition
 First Law of Thermodynamics

Conversion of light energy into glucose by plants

Bioenergetics - the flow of
energy in living systems
First Law of thermodynamics
Energy cannot be destroyed
or created, only transformed.
a. The transformation is
not 100%
Second Law of Thermodynamics

The entropy or disorder of a closed system is always

increasing as the chemical reaction proceeds. More entropy is
generated, less energy is available to do work.
If the chemical reaction generates entropy is irreversible unless
you put more energy to reverses it.
However, humans are not a closed system. We are
exchanging heat with the surroundings and we decreases
entropy at the expense of the entropy of the environment.
Spontaneous process generate entropy
This law relates to endergonic and exergonic
reactions.
Endergonic and Exergonic Reactions

1. Endergonic reactions absorbs energy to

proceed.
2) The reactants/substrates contain less
energy than a final product.
3) Occur in reactions where the reactants are at a
greater state of entropy and the products are at a
lesser state of entropy
Example - plants need the energy from light to
turn carbon dioxide and water into glucose.
Exergonic Reactions

a. Chemical reactions that releases/produce

energy.
b. The substrates/reactants contain more energy
than the product. Products will have less free
energy than the reactants.
c. Example - breaking glucose down into carbon
dioxide and water produces energy.
d. Energy is used to make ATP for use in other
endergonic reactions in the body.
Energy Obtained from Glucose

Substrates have higher energy than the

final product
Coupled Reactions

1. Energy from the environment (food) is broken down in

exergonic reactions to drive the endergonic reactions
in our body.
2. Energy must be stored in a usable form, ATP
a. The production of ATP is an endergonic reaction that is
coupled to an exergonic reaction to drive it.
b. The ATP molecule stores energy in its bonds to be used
elsewhere.
c. ATP is called the universal energy carrier.
d. ADP + Pi 🡺 ATP = Endergonic
e. ATP 🡺 ADP + Pi = Exergonic
Hydrolysis and Condensation:

Hydrolysis: the cleavage of chemical bonds by the

addition of water.
A-B + H2O → A-OH + H-B
(e.g., sucrose + H2O → glucose + fructose)
Condensation:  When two molecules combine to
form a larger molecule, with the loss of water
A-OH + H-B → A-B + H2O
(e.g., glucose + fructose → sucrose + H2O)
Phosphorylation Dephosphorylation

Phosphorylation:  Is the addition of phosphate group (Pi)

group to an organic molecule. 
A + Pi → A-P
(e.g., ADP + Pi → ATP + H2O)
Dephosphorylation: Is the removal of a phosphate group (P)
from an organic compound by hydrolysis
A-P → A + Pi
(e.g., ATP + H2O → ADP + Pi; also a hydrolysis reaction)
Coupled Reactions: Oxidation-Reduction

1. Reduction: when an atom or molecule gains electrons

(is reduced)
a. It is reduced in charge (electrons are negative).
2. Oxidation: when an atom or molecule loses electrons
(is oxidized)
a. Oxygen may not be involved
3. These reactions are always coupled. For one
molecule to lose an electron, it has to give it to another
molecule.
a. Reducing agent: electron donor
b. Oxidizing agent: electron receiver
Oxidation-Reduction = Redox = together

Oxidation Reduction: Is a chemical reaction that involves a

transfer of electrons between two specie
Oxidation = Loss/Removal of electrons
A∙ + B AB∙, where ∙ is an electron
A is oxidized (loses electron)
Reduction = Gain of electron
A∙ + B = AB∙, where ∙ is an electron
B is reduced (gains electron)
(e.g., glucose + 6 O2 → 6 CO2 + 6 H2O)
Oxidation – Reduction, cont

4. Many molecules can be both oxidizers and

reducers in a chain reaction where electrons are
passed along.
5. Oxygen is a great electron acceptor, which is why
the process is called oxidation. Oxygen is not the
only oxidizer
6. Usually, free electrons are not passed along, but
hydrogen atoms carrying the electrons are.
a. A molecule that loses hydrogen is oxidized.
b. A molecule that gains hydrogen is reduced.
Hydrogen carrier molecules

a. NAD = nicotinamide adenine dinucleotide; comes

from the vitamin niacin (B3)
b. FAD = flavin adenine dinucleotide; comes from the
vitamin riboflavin (B2)
c. NAD and FAD are coenzymes that play an
important role in hydrogen transfer mainly in the
electron transport step of full glucose oxidation
Action of NAD