MODULE 5 ENZYMES

Module 4

Module
4
MTCC 117
Enzymes 1
Charisse Anne P. Igaran, RMT

JMJ Marists Brothers

Notre Dame of Marbel University
College of Arts and Sciences
MTCC117/INSTRUCTOR:
MEDICALCHARISSE
TECHNOLOGYANNE PASION IGARAN, RMT
DEPARTMENT 1ST SEMESTER S.Y.2020-2021 1
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Virtually all reactions in the body are mediated by enzymes, which are protein catalysts that increase
the rate of reactions without being changed in the overall process. Among the many biologic reactions that
are energetically possible, enzymes selectively channel reactants (called substrates) into useful pathways.
Enzymes thus direct all metabolic events. This module examines the nature of these catalytic molecules and
their mechanism of action.

LEARNING OBJECTIVES
At the end of the module, the students will be able to:

1. Discuss general characteristics for enzymes in terms of structure and

composition
2. Describe what a substrate is and be familiar with the terminology used to
classify enzymes based on the types of reactions they catalyse.
3. Describe the concept of a “lock and key” and “induced fit” model of
enzyme action.
4. Be able to categorize enzymes in terms of specificity characteristics.
5. Explain how temperature, pH, substrate concentration, and enzyme
concentration affect enzyme activity.

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ABSTRACTION
General Characteristics of Enzymes

• Enzymes are usually proteins that act as biological catalysts.

• Each cell in the human body contains thousands of different enzymes.
• Enzymes cause cellular reactions to occur millions of times faster than corresponding uncatalyzed reactions
• An enzyme speeds a reaction by lowering the activation energy, changing the reaction pathway that provides a
lower energy route for conversion of substrate to product.
• As catalysts enzymes are not consumed in the reactions
• A few enzymes are now known to be ribonucleic acids (RNA)

Enzyme Structure

Simple and Conjugated Enzymes

• Most enzymes are globular proteins; some are simple proteins, others are conjugated proteins

• Simple enzyme: composed only of protein (amino acid chains)

It is the 3o structure of the simple enzymes that makes it biologically active

• Conjugated enzyme: has a non-protein part in addition to a protein part.

1. apoenzyme -protein part; inactive in itself

2. cofactor /coenzyme- nonprotein organic

(coenzyme /co-substrate) or inorganic (cofactor) moiety; the activator; loosely bound to protein

•apoenzyme + cofactor = holoenzyme (biologically active conjugated enzyme)

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Nomenclature and Classification of Enzymes

• Most commonly named with reference to their function

– type of reaction catalyzed
– identity of the substrate
• A substrate is the reactant in an enzyme-catalyzed reaction:
– the substrate is the substance upon which the enzyme “acts.”
– e. g., In the fermentation process, sugar is converted to alcohol, therefore in this reaction sugar is the
substrate

Three Important Aspects of the Naming

Process

1. Suffix -ase identifies it as an enzyme

a. e.g., urease, sucrase, and lipase are
all enzyme designations
b. exception: the suffix -in is still
found in the names of some
digestive enzymes, e.g., trypsin,
chymotrypsin, and pepsin
2. Type of reaction catalyzed by an
enzyme is often used as a prefix
c. e.g., oxidase - catalyzes an
oxidation reaction,
d. e.g., hydrolase - catalyzes a hydrolysis reaction
3. Identity of substrate is often used in addition to the type of reaction
e. e.g. glucose oxidase, pyruvate carboxylase, and succinate dehydrogenase

PRACTICE EXERCISE
1. Predict the function of the following enzymes.
a. Maltase
b. Lactate dehydrogenase
c. Fructose oxidase
d. Maleate isomerase
2. Predict the function of the following enzymes.
a. Maltase
b. Lactate dehydrogenase
c. Fructose oxidase
d. Maleate isomerase

MTCC117/INSTRUCTOR: CHARISSE ANNE PASION IGARAN, RMT 1ST SEMESTER S.Y.2020-2021 4

MODULE 5 ENZYMES

Six Major Classes of Enzymes

• Enzymes are grouped into six major classes based on the types of reactions they catalyse

Class Reaction Catalyzed

1. Oxidoreductases Oxidation-reductions

To help you
2. Transferases Functional group transfer reactions
remember,
3. Hydrolases Hydrolysis reactions

4. Lyases Reactions involving addition of a group

“O-T-H-L-I-L”
to a double bond or removal of groups to
form double bonds

5. Isomerase Isomerization reactions

6. Ligases Reactions involving bond formation

coupled with ATP
hydrolysis

Oxidoreductase
• An oxidoreductase enzyme catalyzes an oxidation–reduction reaction: Up one, down one
– oxidation and reduction reactions are always linked to one another
– an oxidoreductase requires a coenzyme that is either oxidized or reduced as the substrate in the
reaction.
– e.g., lactate dehydrogenase is an oxidoreductase and NAD+ is the coenzyme in this reaction.

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MODULE 5 ENZYMES

Transferase
• A transferase is an enzyme that catalyzes the transfer of a functional group You don’t belong
from one molecule to another here!
• Two major subtypes:
1. kinases - catalyze transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate
2. transaminases - catalyze transfer of an amino group to a substrate

Hydrolase
Water does it again!
• a hydrolase is an enzyme that catalyzes a hydrolysis reaction
• the reaction involves addition of a water molecule to a bond to cause bond breakage
• hydrolysis reactions are central to the process of digestion:
– carbohydrases hydrolyze glycosidic bonds in oligo- and polysaccharides
– proteases effect the breaking of peptide linkages in proteins
– lipases effect the breaking of ester linkages in triacylglycerols

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MODULE 5 ENZYMES

Lyase Taking it apart

• A lyase is an enzyme that catalyzes the addition or the removal of a group
in a manner that does not involve hydrolysis or oxidation
– dehydratase: effects the removal of the components of water to form a double bond
– hydratase: effects the addition of the components of water to a double bond
– decarboxylase: effects the removal of carbon dioxide from a substrate
– deaminase: effects the removal of ammonia from a substrate

Isomerase
• An isomerase is an enzyme that catalyzes the isomerization (rearrangement
of atoms) of a substrate in a reaction, converting it into a molecule isomeric
Shuffling the deck
with itself.
– racemases – conversion of D- to L- isomer or vice versa
– mutases – transfer of a functional group within a molecule

Ligase
• A ligase is an enzyme that catalyzes the formation of a bond between two Putting it together
molecules involving ATP hydrolysis to ADP:
– ATP hydrolysis is required because such reactions are energetically unfavorable
– synthetases – formation of new bond between two substrates with participation of ATP
– carboxylases – formation of new bond between substrate and carbon dioxide with participation of ATP

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MODULE 5 ENZYMES

PRACTICE EXERCISE

To what main enzyme class do the enzymes that catalyze the

following chemical reactions belong?

From the keywords we used to remember the class of

enzymes, try to remember the enzymes with these phrases.

Up one, down one You don’t belong Water does it again!

here!

Putting it together Taking it apart Shuffling the deck

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Models of Enzyme Action

• Enzyme Active Site
• Explanations of how enzymes function as catalysts in
biochemical systems are based on the concepts of an enzyme
active site and enzyme-substrate complex formation.
• The active site: relatively small part of an enzyme’s structure
that is actually involved in catalysis:
– where substrate binds to enzyme
– formed due to folding and bending of the protein.
– usually a “crevice like” location in the enzyme
– some enzymes have more than one active site

Enzyme Substrate Complex

• Intermediate reaction species formed when substrate binds

with the active site
• Needed for the activity of enzyme
• Orientation and proximity is favorable and reaction is
fast

ACTIVITY 1

To help you visualize the enzyme-substrate complex, please copy the link and watch the video,

https://www.youtube.com/watch?v=aRSfPLp_I10

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Two Models for Substrate Binding to Enzyme

• Lock-and-Key model:
– In this model, the active site in the enzyme has a fixed, rigid geometrical conformation
– only substrate of specific shape can bind with active site; a substrate whose shape and chemical nature
are complementary to those of the active site can interact with the enzyme.
– fails to take into account proteins’ conformational changes to accommodate a substrate molecule

• Induced Fit Model:

– substrate contact with enzyme will change the shape of the active site
– allows small change in space to accommodate substrate (e.g., how a hand fits into a glove)
– the enzyme active site, although not exactly complementary in shape to that of the substrate, is flexible
enough that it can adapt to the shape of the substrate.

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Forces That Determine Substrate Binding

• H-bonding
• Hydrophobic
interactions
• Electrostatic
interactions

Enzyme Specificity

• Absolute Specificity:
– an enzyme will catalyze a particular reaction for only one substrate
– this is most restrictive of all specificities (not common)
– e.g., catalase is an enzyme with absolute specificity for hydrogen peroxide (H2O2)
– urease absolute specificity for urea

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• Stereochemical Specificity:
– an enzyme can distinguish between stereoisomers
– chirality is inherent in an active site (amino acids are chiral compounds)
– L-amino-acid oxidase - catalyzes reactions of L-amino acids but not of D-amino acids.
• Group Specificity:
– involves structurally similar compounds that have the same functional groups.
– e.g., carboxypeptidase: cleaves amino acids one at a time from the carboxyl end of the peptide chain
• Linkage Specificity:
– involves a particular type of bond irrespective of the structural features in the vicinity of the bond
– considered most general of enzyme specificities
– e.g., phosphatases: hydrolyze phosphate–ester bonds in all types of phosphate esters

Factors That Affect Enzyme Activity

Enzymes can be isolated from cells and their properties studied in a test tube (that is, in vitro). Different enzymes
show different responses to changes in substrate concentration, temperature, and pH. This section describes factors
that influence the reaction velocity of enzymes. Enzymic responses to these factors give us valuable clues as to how
enzymes function in living cells (that is, in vivo).

Enzyme Activity
• A measure of the rate at which enzyme converts
substrate to products in a biochemical reaction
• Four factors affect enzyme activity:
o Temperature
o pH
o Substrate concentration
o Enzyme concentration

Temperature
• Higher temperature results in higher kinetic energy which
causes an increase in
number of reactant collisions, therefore there is higher
activity.
• Optimum temperature: temperature at which the rate of
enzyme- catalyzed
reaction is maximum
• Optimum temperature for human enzymes is 37ºC (body
temperature)
• Increased temperature (high fever) leads to decreased
enzyme activity

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pH
• Drastic changes in pH can result in denaturation of proteins
• Optimum pH: pH at which enzyme has maximum activity
• Most enzymes have optimal activity in the pH range of 7.0 - 7.5
• Exception: digestive enzymes
– pepsin: optimum pH = 2.0
– trypsin: optimum pH = 8.0

Substrate Concentration
• At a constant enzyme concentration, the enzyme
activity increases with
increased substrate concentration.
• Enzyme saturation: the concentration at which it
reaches its maximum
rate and all of the active sites are full
• Turnover number: number of substrate molecules
converted to product
per second per enzyme molecule under
conditions of optimum temperature and pH

Enzyme Concentration

• Enzymes are not consumed in the reactions they

catalyze
• At a constant substrate concentration, enzyme
activity increases with
• increase in enzyme concentration
– the greater the enzyme concentration, the
greater the reaction rate.

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MODULE 5 ENZYMES

Practice Exercise
• Describe the effect that each of the following changes would have on the rate
of a reaction that involves the substrate sucrose and the intestinal enzyme sucrase.
o Decreasing the sucrase concentration
o Increasing the sucrose concentration
o Lowering the temperature to 10ºC
o Raising the pH from 6.0 to 8.0 when the optimum pH is 6.2

SUPPLEMENTARY ACTIVITY
Copy the link and watch this video and appreciate how enzymes work!

https://www.youtube.com/watch?v=yk14dOOvwMk

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