Enzyme:

biological
catalyst
GROUP 3
GROUP 3
Aurellano, wighie
gelido, mary austine
fernandez, John luis
licudan, astrid
mabbun, kyla mae
ong, Bieniley rose
TABLE OF CONTENTS
01 introduction

02 History

03 general properties

04 CLASSES OF ENZYMES

05 NOMENCLATURE OF ENZYMES

06 REGULATORY OF ENZYMES

07 REGULATION OF ENZYME ACTIVITY

01
INTRODUCTION
WHAT ARE ENZYMES?
Enzymes are highly specialized types of
proteins.

Enzymes are central to every biochemical

process.
02
HISTORY
In the 1850s, Louis Pasteur concluded that fermentation of sugar into
alcohol by yeast is catalyzed by "ferments." He postulated that these
ferments were inseparable from the structure of living yeast cells; this
view, called vitalism, prevailed for decades

Then in 1897, Eduard Buchner discovered that yeast extracts could

ferment sugar to alcohol, proving that fermentation was promoted
by molecules that continued to function when removed from cells.
Buchner's experiment at once marked the end of vitalistic notions
and the dawn of the science of biochemistry.

Frederick W. Kuhne later gave the name “enzymes"

to the molecules detected by Buchner.
 The isolation and crystallization of urease by James Sumner in 1926
was a breakthrough in early enzyme studies. Sumner found that
urease crystals consisted entirely of protein, and he postulated that all
enzymes are proteins. In the absence of other examples, this idea
remained controversial for some time.

Only in the 1930s was Sumner's conclusion widely accepted,

after John Northrop and Moses Kunitz crystallized pepsin,
trypsin, and other digestive enzymes and found them also to be
proteins.
 During this period, J. B S. Haldane wrote a treatise entitled
Enzymes. Although the molecular nature of enzymes was not
yet fully appreciated, Haldane made the remarkable suggestion
that weak bonding interactions between an enzyme and its
substrate might be used to catalyze a reaction. This insight lies
at the heart of our current understanding of enzymatic catalysis.

Since the latter part of the twentieth century thousands of enzymes have been
purified, their structures elucidated, and their mechanisms explained.
03
GENERAL
PROPERTIES
 GENERAL PROPERTIES
1. SPECIFICITY
Most enzymes will catalyze only a specific range of reactions,
and in many cases only one reaction will be catalyzed by a
given enzyme. Some enzymes have a low degree of specificity.
Pepsin hydrolyzes almost all soluble native proteins, but
the hydrolysis is limited to certain very specific peptide
linkages.
Urease is a highly specific enzyme; its only known
substrate is urea.
Arginase acts only on L-arginine; it does not attack D-
arginine.
 GENERAL PROPERTIES
2. HIGHER REACTION RATE
Enzymes are exceedingly efficient. Most enzymatic reactions,
under optimal conditions, proceed 10^8 to 10^11 times more
rapidly than the corresponding non enzymatic reactions.

3. BIOLOGICAL CATALYST
Enzymes as a group are exceptionally versatile catalysts.
For example, they effectively catalyze hydrolytic
reactions, dehydrations, acyl transfer reactions,
oxidation-reduction reaction, polymerizations, aldol
condensations, and free-radical reactions.
 GENERAL PROPERTIES
4. CELLULAR CONTROLS
Enzymes are subject to a variety of cellular controls. Their final
concentration and rate of synthesis are under genetic control.
In addition, enzymes can be present in the cell in both inactive
to active forms. The rate of conversion from inactive to active
form is influenced by environmental changes.
Phosphorylase b is converted to phosphorylase a very
rapidly through a series of reactions that are triggered by
the release of catecholamines.
04
CLASSES OF
ENZYMES
 CLASSES OF ENZYMES
enzyme Typical reaction
→ A + BH (reduced)
AH + B
Oxidoreductase
A+0 → A0 (oxidized)
Transferases AB+C→A+ BC

Hydrolases AB + H20 → AOH + BH

 CLASSES OF ENZYMES
enzyme Typical reaction
RCOCOOH → RCOH + CO2
Lyases or
[X-A-B-Y] → [A=B + X-Y]

Isomerases AB → BA

Ligasws X + Y+ ATP → XY + ADP + Pi

 OXIDOREDUCTASE
Number: 1
Type of Reaction: Redox Reaction
Examples: Lactate dehydrogenase,
peroxidases
 OXIDOREDUCTASE

Biochemical Properties
These are enzymes that catalyze the redox
reaction, thereby facilitate the electron
transfer. (dehydrogenase peroxidase)
 TRANSFERASES
Number: 2
Type of Reaction: Group Transfer
Examples:
Kinase-phosphate transfer
Transaminases-amino group
transfer
 TRANSFERASES
Biochemical Properties
Catalyze the transfer of functional groups that contains C,
N, & P between donor and acceptor molecules. Kinases
are specialized transferases that regulate metabolism by
transferring phosphate from ATP to other molecules;
Transaminases-transfer of amino group).
 HYDROLASES
Number: 3
Type of Reaction:
Hydrolysis reaction
Transfer of functional group to water
Examples: Lipases, proteases, amylases
and phosphatases
 HYDROLASES
Biochemical Properties
Catalyzes the hydrolysis of certain compounds
which results in the breaking of bonds lipases,
proteases, amylases and phosphatases.)
 LYASES
Number: 4
Type of Reaction: Addition or removal of
groups to form double bond
Examples: Fumarase
 LYASES
Biochemical Properties
Addition or removal of groups to form
double bond
 ISOMERASES
Number: 5 Examples:
Type of Reaction: Triose phosphate
Isomerization reaction Isomerase
Intermolecular group transfer
Cis to Trans
D to L
Aldehyde to ketose
 ISOMERASES
Biochemical Properties

Carry out many kinds of isomerization:

L to Disomerization
cis to trans isomerization
mutase reactions.
 LIGASES
Number: 6
Type of Reaction:
Litigation or joining of two chemical substrates
at the expense of ATP hydrolysis
Example: Aminoacyl tRNA synthetase
 LIGASES
Biochemical Properties
Catalyze reactions in which two chemical
groups are joined (or ligated) with the use of
energy from АТР. (formation of bonds
between C and oxygen, sulfur and nitrogen)
05
NOMENCLATURE
OF ENZYMES
The nomenclature was determined by the Enzyme Commission in 1961

All enzymes are assigned an “EC” number. The classification does not take into
account amino acid sequence (ie, homology), protein structure, or chemical
mechanism

EC numbers are four digits, for example a.b.c.d, where “a” is the class, “b” is the
subclass, “c” is the sub-subclass, and “d” is the sub-sub-subclass. The “b” and “c” digits
describe the reaction, while the “d” digit is used to distinguish between different
enzymes of the same function based on the actual substrate in the reaction.

Enzymes are classified into six different groups according to the reaction being
catalyzed.

Most common name of an enzyme have the suffix “ase” attached to the substrate that
interacts with the enzymes.
6 PRINCIPAL
CATEGORIES AND
THEIR REACTIONS:
 EC1.
OXIDOREDUCTASE
which are involved in electron transfer
– catalyze the transfer of hydrogen or oxygen atoms or
electrons from one substrate to another, also called
oxidases, dehydrogenases, or reductases.
Note that since these are ‘redox’ reactions, an electron
donor/acceptor is also required to complete the
reaction.
 EC2. TRANSFERASE

which tansfer a chemical group from one substance

to another
catalyze group transfer reactions, excluding
oxidoreductases (which transfer hydrogen or oxygen
and are EC 1). These are of the general form:

A-X + B ↔ BX + A
 EC3. HYDROLASE

which cleave the substrate by uptake of a water

molecule (hydrolysis)
catalyze hydrolytic reactions. Includes lipases,
esterases, nitrilases, peptidases/proteases. These are
of the general form:

A-X + H2O ↔ X-OH + HA

 EC4. LYASE

which form double bonds by adding or removing a chemical

group
catalyze non-hydrolytic (covered in EC 3) removal of
functional groups from substrates, often creating a double
bond in the product; or the reverse reaction, ie, addition of
function groups across a double bond. Includes
decarboxylases and aldolases in the removal direction, and
synthases in the addition direction.
 EC5. ISOMERASE

which transfer a group within a molecule to form an

isomer
catalyzes isomerization reactions, including
racemizations and cistran isomerizations.
 EC6. LIGASE

or synthetases, which couple the formation of various chemical

bonds to the breakdown of a pyrophosphate bond in adenosine
triphosphate or a similar nucleotide
catalyzes the synthesis of various (mostly C-X) bonds, coupled
with the breakdown of energy-containing substrates. ATP The
various sub-classes are defined based on the primary class.
The function of the enzyme is generally conveyed
directly by its common name.
E.g, sucrase, urase, dehydrogenase

Some enzymes retained their trivial name which

gives no hint of the associated enzymatic activities.
-Pepsin, trypsin, and chymotrypsin.
Pepsin – endopeptidase that breaks down
proteins into smaller peptides.
Trypsin – form from small intestine, hydrolyzes
protein at carboxyl side of a lysine and arginine.
Chymotrypsin – hydrolyze peptide bonds
formed by the carboxyl group of try, phe, trp,
and leu.
Trypsinogen – release from pancreas inactive
form activated along duodenum into trypsin.
06
MODES AND FACTORS
THAT AFFECT
ENZYME ACTIVITY
1. Enzyme Concentration
The transient bonds between enzymes and their substrates
catalyze the reactions by decreasing the activation energy and
stabilizing the transition state. Given the exceeding amount of
substrates and the necessary cofactors, enzymatic reactions
possessing higher enzyme concentrations will reach equilibrium
before those with the same enzyme but at lower concentrations.
2. Substrate Concentration
An enzyme’s activity increases with the rise in substrate
concentration. The enzyme activity rises until it reaches a
maximum limit.
In other words, the enzyme molecules are completely saturated
with the substrate. This means that all enzymes’ active sites are
occupied. The surplus substrate molecules will not react until the
substrate that has already been bound to the enzymes has
reacted and has been released or released without reacting.
2. Substrate Concentration
3. PH VALUE
pH has an impact on enzyme activity. A bell-shaped curve
emerges when enzyme activity is plotted versus pH. Each
enzyme has a certain optimal pH at which the reaction rate is the
fastest. The optimal pH is when a specific enzyme’s activity is at
its peak. The enzyme activity is greatly reduced below and above
the optimal pH, and at high pH, the enzyme becomes completely
inactive.
3. PH VALUE
 4. TEMPERATURE
An optimum temperature range is required to maximize the
enzyme activity. Temperatures that are either higher or lower than
the optimal temperature causes a decrease in the enzyme activity
and can lead to denaturation (when the temperature is too high).

The temperatures between 37 and 45 are referred to as the optimal temperature

for most enzymes. At this given temperature, most enzymes become more active.
Extremely high temperatures can cause an enzyme to lose its denature form and
eventually stop functioning. The majority of enzymes in the human body have a
temperature optimum of 37 °C and are denatured or destroyed at higher
temperatures.
4. TEMPERATURE
5.Enzyme inhibitors and activators
Activators also known as (co-enzymes), such as metal ions, are
required for optimal enzyme activity.

The chloride ion, for example, is required for amylase to operate.

Amylase is a digestive enzyme secreted by the pancreas and
salivary glands also found in other tissues in very small quantities.
Metal ions or cofactors, for example, are required to regulate or
initiate the catalytic activity of several enzymes.
 Depending on the inhibition kinetics,
enzyme inhibition can be classified as:

IRREVERSIBLE INHIBITION
AND
REVERSIBLE INHIBITION.
 Irreversible inhibitors
Irreversible inhibitors bind to an enzyme in a strong covalent
connection. These inhibitors might act on the active site, close
to it, or far away. As a result, adding more substrate may not be
enough to eliminate them. In either event, the enzyme’s basic
structure is altered to the point that it no longer functions.
 Reversible inhibitors

In reversible inhibition, the inhibitor rapidly dissociates from

the enzyme-inhibitor complex.
 There are three types of
reversible inhibitions:
1.COMPETITIVE
2.NON-COMPETITIVE
3.UNCOMPETITIVE (ANTI-COMPETITIVE)
Competitive inhibition
When an inhibitor and a substrate bind to the enzyme in a competitive
way, this is known as competitive inhibition. Any molecule with a
chemical structure and molecular geometry similar to the substrate could
be used as a competitive inhibitor.
Contacts between the inhibitor and the enzyme in the active site may be
strong. Still, no reaction will occur since the inhibitor does not have the
same chemical reactivity as the enzyme, eventually lowering the reaction
rate. Competitive inhibition is usually temporary and reversible.
Competitive inhibition
Non-competitive inhibitors
Non-competitive inhibitors bind to the enzyme at a different location, causing the
active site to change shape and prevent the substrate from binding to it. During
non-competitive inhibition, the enzyme may form complexes with either the
substrate, the inhibitor, or both.
Allosteric inhibition is non-competitive inhibition because the inhibitor binds to the
allosteric site rather than the active site. Binding to an allosteric site causes the
enzyme’s 3-dimensional tertiary structure to be distorted, preventing it from
catalyzing the process. Because they effectively denature the enzymes, some non-
competitive inhibitors are irreversible and permanent.
Non-competitive inhibitors
Uncompetitive inhibition
Uncompetitive inhibition is a rare occurrence. An
uncompetitive inhibitor binds to the enzyme and increases the
substrate’s binding affinity, but the resulting enzyme-inhibitor-
substrate complex reacts slowly to create the product.
Note that before binding to the inhibitor, uncompetitive
inhibition necessitates the creation of an enzyme-substrate
complex.
07
REGULATION OF
ENZYME ACTIVITY
 REGULATORY ENZYMES
Regulatory enzymes exhibits increased or decreased
catalytic activity in response to certain signals
In most multienzyme systems, the first enzyme of the
sequence is regulatory enzymes. This is an excellent place
to regulate a pathway, because catalysis of an unneeded
products diverts energy and metabolite from more
important process.
 THE TWO MAJOR
MECHANISMS OF
CONTROLLING ENZYMES ARE:

Allosteric Enzymes
Covalent Modification
ALLOSTERIC ENZYMES
Allosteric proteins are those having "other shapes" or
conformations induced by the binding of modulators.
Function through reversible, non covalent binding of
regulatory compound called allosteric modulators or
allosteric effectors.
The modulators for allosteric enzymes may be
inhibitory or stimulatory
Allosteric (noncovalent) regulation may permit fine-
tuning of metabolic pathways that are required
continuously but at different levels of activity as
cellular condition change.
COVALENT MODIFICATION
In covalent modification, a functional group is
transferred from one molecule onto the enzyme or
protein, thereby turning the enzyme either on or
off. Although there are many types of covalent
modifications, one common form is called
phosphorylation.
Regulation by covalent modification may be all or
none. usually the case with proteolytic cleavage or it
may allow for subtle changes in activity.
REGULATED STEPS ARE CATALYZED BY
ALLOSTERIC ENZYMES:
When the regulatory enzymes reaction is slowed,
subsequent enzymes may operate at different rates of as
their substrate pools are depleted. The rate of the
production of the pathway's end product is thereby
brought into balance with cell's need. This type of
regulation is called FEEDBACK INHIBITION.

One of the first known examples of allosteric feedback

inhibition was the bacterial enzyme system that catalyzes
the conversion of L-threonine to L-isoleucine in five
steps.
FEEDBACK INHIBITION
Allosteric inhibition is called feedback inhibition
because in feedback inhibition, the end products of
a reaction are known to bind to the allosteric site of
the enzyme leading to the inactivation of enzyme
thereby producing a lesser amount of products.
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