President Ramon Magsaysay State University

College of Arts and Science

Biology Department

Cell and Enzymes

By:
BRANDON M. ESTIGOY, LPT
Early Discoveries of Enzymes
• 1835 by the Swedish chemist, Jon Jakob Berzelius who termed their
chemical action catalytic
• 1926 – James B. Sumner (Nobel Prize 1947) of Cornell University
was able to isolate and crystallized the first enzyme – “UREASE”
• John H. Northrop and Wendell M. Stanley of the Rockefeller Institute
for Medical They discovered a complex procedure for isolating and
purifying pepsin.
• Enzyme is derived from the Greek words en (meaning ‘within’) and
zume (meaning ‘yeast’) by Wilhelm Kühne in 1878
Enzymes
• Enzymes are biological
catalysts that convert a
substrate to a product
• Enzymes are large
protein molecules that
increases the rates of
chemical reaction
without themselves
undergoing change.
Enzymes
• Most enzymes are proteins but there are a few RNA enzymes,
called ribozymes.
• Some protein enzymes also contain metals as part of their structure
or are involved in catalysis; these enzymes are called
metalloenzymes.
• Enzymes speed up the conversion of a substance, called its
substrate to another substance(s) called the product.
• Enzymes can be denatured and precipitated with salts, solvents and
other reagents.
• Enzymes have molecular weights ranging from 10,000 to 2,000,000
Da.
 Enzymes
• Enzymes are globular with a
small hydrophobic pockets
(a cavity within the enzyme
molecule where substrates
bind).
• This cavity is the enzyme’s
active or catalytic site.
• When enzymes bind the
substrate, an intermediate
called the enzyme-substrate
complex (ES) is formed.
Chemical Natures of Enzymes
Chemical Natures of Enzymes
• Enzymes need only proteins in their structure for their
activity, however, many enzymes require the presence of
other compounds – cofactors – before their catalytic activity
can be exerted.
• This entire active complex is referred to as the
holoenzyme; i.e., apoenzyme (protein portion) plus the
cofactor(s) (coenzyme, prosthetic group or metal-ion
activator)
Enzymes
According to Holum, the cofactor may be:
1. A coenzyme – a non-protein organic substance which
is dialyzable, thermostable and loosely attached to the
protein part.
2. A prosthetic group – an organic substance which is
dialyzable and thermostable which is firmly attached to
the protein or apoenzyme portion.
3. A metal-ion-activator – these include K+, Fe2+, Fe3+,
Cu2+, Co2+, Zn2+, Mn2+, Mg2+, Ca2+, and Mo3+.
Holoenzymes
Example of a CoEnzyme:
ENZYMATIC REACTION
• The compound on which the enzyme works and whose
reaction is being speed up is called the substrate.
• An enzymatic reaction begins with the substrate binding
at a specific location called the active site.
Enzyme catalysis proceeds as follows:
• According to the theory of Savante Arrhenius in 1888,
where in the substrate and enzyme formed some
intermediate substance which is known as the
enzyme/substratecomplex (ES)
Nomenclature of Enzymes
Name an Enzymes
• The International Union of Biochemistry and Molecular
Biology (I.U.B.M.B) initiated standards of enzyme
nomenclature which recommended that enzyme names
indicate both the substrate acted upon and the type of
reaction catalyzed.
• The main group classification of enzymes is based on
similarities in the reactions they catalyzed.
• These groups are: 1) oxidoreductases; 2) transferases; 3)
hydrolases; 4) lyases; 5) isomerases and 6) ligases.
Name an Enzymes

• OXIDOREDUCTASES. These are enzymes that catalyze

redox reactions or oxidation-reduction reactions.
• TRANSFERASES. These enzymes catalyze the transfer
of groups from a donor to a receiver.
• HYDROLYSES are enzymes that catalyze the cleavage
of bonds (C-O, C-C, C-N, O-P, etc.) with the participation
of water.
Name an Enzymes
• LYASES are enzymes that cleave bonds (C-O, C-C, C-N,
etc.) without water as participant in the reaction and by
elimination. The products usually contain double bonds
or form cyclic structures.
• ISOMERASES – These enzymes catalyse geometric or
structural changes within one molecule. According to the
type of isomerism, they may be called racemases,
epimerases, cis-trans-isomerases, isomerases,
tautomerases, mutases or cycloisomerases
Name an Enzymes
• LIGASES are enzymes that catalyze the joining together
of two molecules coupled with the hydrolysis of
compounds with high-energy transfer potential such as
the hydrolysis of ATP.
• TRANSLOCASES – Catalysing the translocation of
hydrogen ions, inorganic cations and anions, amino
acids, carbohydrates or other compounds. A new EC
class was created in 2018
 With many enzymes in nature, there are
always exceptions to the general rules. Many
common names are still being used today
such as trypsin, pepsin, etc. as
these are already known to all.
PROPERTIES OF ENZYMES
ENZYMES EFFIENCY
• Enzymes are
NATURE’S CATALYST,
converting substrate to
product efficiently and
at astonishing rates.
ENZYMES CATALYSIS
Enzymes as a CATALYST
• Substance that can be added to a reaction to increase
the reaction rate without getting consumed in the
process
• Speed up a reaction by reducing the activation energy
or changing the reaction mechanism.

Ex. Regulation of blood pH by Carbonic anhydrase

Properties of a Catalyst

1. They are active at very low concentrations within

the cell;
2. They increase the rate of reactions but they
themselves are not altered in the process;
3. They do not change the nature of the products.
ENZYMES as a catalyst:
1. Enzyme as catalyst are extremely effective by
increasing the reaction rates from 109 to 1020 times.
2. Enzyme as catalyst are extremely specific, that is,
each of them speeding up only one particular
reaction or class of reactions.
ENZYMES SPECIFICITY:
• LOCK and KEY
- Enzyme proteins are
made up of amino acid
chains that fold to create
a hydrophobic pocket that
shows complementarity
with its substrate, as a
key fits to the lock.
LOCK AND KEY MODEL
 INDUCED FIT
- Enzyme-substrate interaction to
describe that the substrate is
capable of inducing the proper
alignment of the active site of the
enzyme, causing the latter to
subsequently perform its catalytic
function.
INDUCED FIT MODEL
ENZYMES are Sensitive to Nature
• Enzymes, being a biomolecule, are affected by
alterations in environmental pH and temperature.
• These are constraints that biological systems have,
i.e. it must maintain a physiological pH of 6.7 to 7.4
and a temperature range of 36-37oC.
ENZYMES are TRUE Catalyst
• Enzymes are true catalysts, in that while they increase
reaction rates, they do so without themselves being altered
in the process.
• Enzymes also do not alter the equilibrium constants of
reactions they catalyze.

A B
• Many biological pathways are made up of linked series of
dependent reactions.
• Each reaction is catalyzed by enzymes whose product is
the substrate of the next enzyme.
• The products formed in the series, except the end product,
are called intermediates.
• The quality and quantity of the end product however, is
dependent on the efficiency of every enzyme in the
pathway.
• To ensure this, enzymes are localized near each other so
that intermediates do not accumulate and are immediately
removed or acted upon by the next enzyme.
Like other catalysts, these biological catalysts also lower the energy
of activation of the reaction it catalyzes. But unlike chemical
catalysts, the rate of reactions catalyzed by enzymes is several
hundredfold faster than ordinary chemical reactions. Enzymes are
also not consumed and are regenerated after the reaction.
ALLOTERIC REGULATION
• Most protein enzymes are made up of several
polypeptide chains, i.e. they are multimeric.
• Thus enzyme activity is subject to regulation in
response to concentrations of substrates and other
molecules that bind to allosteric sites of the
enzyme.
Factors Affecting Enzyme Activity
Enzymes Concentration
• Increasing enzyme concentration will speed up the
reaction, as long as there is substrate available to
bind to.
Substrate Concentration
Increase the concentration of the substrate will results
into a point where:
 the rate stays the same even with increase
substrate concentration called as the saturation
point
 at saturation point, substrate molecules are
bound to all available active sites of an enzyme.
Temperature
• Raising temperature generally speeds up a reaction, and lowering
temperature slows down a reaction. However, extreme high
temperatures can cause an enzyme to lose its shape (denature) and
stop working.
pH
• Raising temperature generally speeds up a reaction, and
lowering temperature slows down a reaction.
• However, extreme high and extreme low temperatures
can cause an enzyme to lose its shape (denature) and
stop working.
Effects of Inhibitors on Enzyme
Activity
Competitive Inhibition
• Competitive inhibition occurs when the substrate and a
substance resembling the substrate are both added to
the enzyme
Non-Competitive Inhibition
Substrate Inhibition
THANK YOU!!!