ENZYMES

OBJECTIVES AND GOALS

01. DEFINE AND CLASSIFY ENZYMES.

02. EXPLAIN THE FACTORS INFLUENCING ENZYME ACTIVITY.

03. DESCRIBE THE MECHANISMS OF ENZYME ACTION.

04. UNDERSTAND ENZYME REGULATION AND ITS SIGNIFICANCE.

05. IDENTIFY MEDICAL APPLICATIONS OF ENZYMES, INCLUDING

DESIGNER ENZYMES.
 ENZYMES
Enzymes are protein synthesis
in the living cells, specialized to
catalyze biological reactions.
 ENZYMES
Enzymes are biological catalysts
produced by the captivity of living
organisms such as plants, animals,
and microorganisms - and which
modify the speed of reaction
without being used up or appearing
as one of the end products.
 CHEMICAL NATURE OF
ENZYMES
All enzymes isolated and studied were proven to be proteins.
In general, they are soluble in water, glycerol and diluted
alcohol.
They are precipitated by protein precipitants like
concentrated alcohol, ammonium sulfate and trichloroacetic
acid.
In solution, they are colloidal in nature and are non-
dialyzable.
 BIOLOGICAL IMPORTANCE OF
ENZYMES
Most chemical reactions of living matter are accelerated by
enzymes.
A given cell could contain a thousand different enzymes.
For every organic compound which occurs in nature, there is also
an enzyme capable of reacting with it.
Enzymes are responsible for the different reactions in living matter.
Synthesis, oxidation, hydrolysis, tautomeric changes - necessary
during digestion, metabolism, respiration, energy release, and
energy transfer in all metabolic reactions.
It is not an exaggeration to say that life is impossible without
enzymes.
 NOMENCLATURE (NAMING) OF
ENZYMES
The present convention of naming enzymes is based on:
A. Upon the substance they act upon. The suffix “ase” is
added to the name of the substance.

Urease
Lipase
 NOMENCLATURE (NAMING) OF
ENZYMES
B. Upon the reaction enhanced. The suffix “ase” is also
added to the type of chemical reaction activated.

Oxidation
Removal of CO2 (decarboxylation)
Transamination
Hydrolysis
Hydration
 NOMENCLATURE (NAMING) OF
ENZYMES
C. The first enzyme discovered and studied were given
names that do not indicate the substance acted on or
reaction enhanced;

Among these enzymes are pepsin, trypsin, ptyalin, and

rennin.
 CLASSIFICATION OF ENZYMES
Hydrolases - hydrolysis. Ex. Estrases, Peptidases, Amidases,
Glycosidase, etc.
Desmolases or Lyases - add or remove Ex. Hydrases, Dehydrases,
Decarboxylases, Deaminases.
Transferases - transfer Ex. Transamidases, Transaminases,
Transpeptidases
Oxido-reductases - oxidation and reduction Ex. Oxidases,
Reductases, Dehydrogenases, Hydroxylases
Ligases - bond formation Ex. Synthetases, Carboxylases,
Isomerases - intramolecular arrangement. Ex. Epimerases
 ENZYME TERMINOLOGIES
SUBSTRATE
It is a substance or molecule that an enzyme acts upon to create a product.
Starch is the substrate of amylases.

ZYMOGEN (PROENZYME)
An inactive precursor of an enzyme, also known as a proenzyme.
It is an inactive substance which is converted into an enzyme when
activated by another enzyme.
It also requires a biochemical change to become an active enzyme.

Ex. Pepsin (active form) is secreted as pepsinogen (stomach). Trypsin is

secreted as trypsinogen (intestines)
ACTIVATOR
An activator is a molecule that positively regulates an enzyme's activity.
This term is applied to substances that convert a proenzyme or zymogen
(inactive form) into the active enzyme.
Activators may be inorganic substances or organic in nature.
Organic activators are also called KINASES.

CO-ENZYME
It is defined as an organic molecule that binds to the active sites of certain
enzymes to assist in the catalysis of a reaction.

APO-ENZYME
It is the inactive form of the enzyme, lacking the necessary cofactor or
coenzyme. Apoenzymes also depend on cofactors (metal ions or
coenzymes) to become active.
HOLO-ENZYME
The combination of the Apo-enzyme and coenzyme.
It also refer to enzymes that have multiple protein subunits, where the
holoenzyme is the complete complex that contains all the subunits needed
for activity.

Ex. DNA polymerase and RNA polymerase

ANTI-ENZYME
An anti-enzyme is a substance that prevents or counteracts the action of an
enzyme.

Ex. Anti-trypsin
FACTORS THAT INFLUENCE ENZYME
ACTIVITY
PHYSICAL FACTORS
Substrate Concentration: Increased substrate initially boosts
reaction rate, plateauing when enzymes are saturated.

Enzyme Concentration: Higher enzyme concentration directly

increases reaction rate (given enough substrate).

pH's Effect: Enzymes have optimal pH ranges; deviations reduce

or eliminate activity.
Cofactor Concentration: Many enzymes need cofactors;
insufficient levels limit activity.

Product Effects: Products can influence activity through

substrate consumption, equilibrium shifts, pH changes, or
direct enzyme inhibition.

Time: Reaction rate decreases over time as substrate is

consumed and product accumulates.

Radiation: Radiation can damage enzymes, reducing or

eliminating their activity.
 MECHANISMS OF ENZYME ACTION
Simple Enzyme Action (enzyme-substrate combination)
This theory was proposed by Michaelis and Menten.
Simple enzyme action involves a single substrate being acted upon by
the enzyme to produce a single product.

Simple Enzyme Action Involves:

Substrate Binding
Catalysis
Formed Product
Releasing
 MECHANISMS OF ENZYME ACTIVITY
Complex Enzyme Action involves more intricate interactions, such as:
Multi-substrate reactions.
Cofactor or coenzyme assistance.

Complex Enzyme Action Involves:

Substrate Binding
Cofactor/Coenzyme Involvement
Reaction and Product Formation
Release and
Recycling
 ENZYME REGULATION
Enzyme regulation is the process of controlling the activity of enzymes,
which are catalysts that regulate chemical reactions.

There are multiple ways to regulate enzymes, including:

Competitive Inhibition: An inhibitor molecule binds to the active sit
an enzyme, preventing the substrate from binding.

Non-Competitive Inhibition: this is brought about by the presence o

substances that bring about chemical changes in the enzyme.
 ENZYME REGULATION
Non-Competitive Inhibition includes:

Oxidation-reduction effect - the sulhydryl radical in many enzymes when

oxidized to disulfide (-S-S-) by the removal of hydrogen, renders the enzyme
inactive.
Formation of substances resulting from the action of the inhibitors on co-
factors of the enzyme. This means that the inhibitor reacted with the
coenzyme prosthetic group of the enzyme or ion activator. Decarboxylases
are inhibited by cyanides, hydrazine and semi-carbamide.
Heavy Metals - salts of heavy metals like those of Ag, Pb, Hg are inhibitors.
They probably precipitate the enzymes thus rendering them inactive.
 ENZYMES USED IN MEDICINE
Enzymes are used in medicine for a variety of purposes, including treating
medical conditions, enzyme deficiencies, and as digestive aids:
Asparaginase
Breaks down the amino acid asparagine, which can prevent cancer cells from
synthesizing protein.
Streptokinase
A thrombolysis medication used to treat myocardial infarction and
pulmonary embolism.
Amylase
Used in the preparation of fermented foods and in biopharmaceutical
applications.
Nattokinase
A digestive enzyme that can be used as a blood thinner and blood clot
dissolver.
 ENZYMES USED IN MEDICINE
Collagenase
A topical ointment that breaks up and removes dead skin and tissue,
which can help antibiotics work better and speed up healing.
Bromelain
A mixture of enzymes extracted from pineapples and some fruits and
stems that is used to digest proteins.

Enzymes are used in medicine because they are catalytic, meaning they can
convert multiple target molecules into the desired products. They also bind
and act on their targets with great affinity and specificity.
 ENZYMES USED IN MEDICINE
DESIGNER ENZYMES
Designer enzymes are protein enzymes that are created using an artificial
selection process to perform specific functions.
Designer enzymes can deactivate pathogenic biological agents.
Designer enzymes can be used to create more effective medications.
Designer enzymes can be used in a wide range of chemistry, including
many synthetic applications.
THANK YOU
VERY MUCH!