GROUP 6

"ENZYME"
BAITO, ALISTAIR JAN PAGOTA, KRISTINE FE
LEADER SECRETARY

DIAMANTE, NEIL JUSTINE

REPORTER

NOTADA, AJ HOPE NAMBONG, RACHEL ANN

MEMBER MEMBER

OJARLIZA, KYLA NOVIE PALMES, ALEXI MARGUERITTE

MEMBER MEMBER
OBJECTIVES:
1. Describe Enzyme as well as its structure
2. Determine the functions and uses of Enzymes
3. Describe how Cell utilizes enzymes to speed up
chemical reactions
4. Determine how Cofactors and Co-enzymes
affect Enzyme activity
5. Determine how environmental factors affect
enzyme activity
 ICE
BREAKER
DIRECTIONS:
•You will be given a number which you will
decipher through texting with a basic phone
•Each repetitive digit corresponds to how
many times you will tap a specific key
repeatedly
•Each tap correspond to a letter, and you
must form a specific word that will connect
with the description to be presented
Sample
Is a pocket-like structure
that holds the substrate.
2 222 8 444 888 33
7777 444 8 33

active site
Question 1
A linear chain of amino
acids which functions as a
catalyst

33 66 9999 999 6 33
Question 1
A linear chain of amino
acids which functions as a
catalyst

33 66 9999 999 6 33

ENZYME
 Question 2
It is a substance acted
upon by an enzyme.

7777 88 22 7777 8
777 2 8 33
 Question 2
It is a substance acted
upon by an enzyme.

7777 88 22 7777 8
777 2 8 33

SUBSTRATE
 Question 3
a substance that increases the rate of a
chemical reaction without itself
undergoing any permanent chemical
change.

222 2 8 2 555 999

7777 8
 Question 3
a substance that increases the rate of a
chemical reaction without itself
undergoing any permanent chemical
change.

222 2 8 2 555 999

7777 8

CATALYST
 Question 4

Catalyze the Hydrolysis of A bond

44 999 3 777 666 555

2 7777 33 7777
 Question 4

Catalyze the Hydrolysis of A bond

44 999 3 777 666 555

2 7777 33 7777

hydrolases
 Question 5
increased the enzymes and substrate
gain kinetic energy

8 33 6 7 33 777 2 8 88
777 3
 Question 5
increased the enzymes and substrate
gain kinetic energy

8 33 6 7 33 777 2 8 88
777 3

temperature
 Question 6
These Catalyze Oxidation And Reduction
Reactions

666 99 444 3 666 777

33 3 88 222 8 2 7777
333 7777
 Question 6
These Catalyze Oxidation And Reduction
Reactions

666 99 444 3 666 777

33 3 88 222 8 2 7777
333 7777
Oxidoreductases
 Question 7
Helper Molecules that do not bind the
enzyme

222 666 333 2 222 8

666 777
 Question 7
Helper Molecules that do not bind the
enzyme

222 666 333 2 222 8

666 777

co factor
 WHAT
ARE
ENZYMES?
 ENZYME
ALL BIOLOGICAL
PROCESSES IN LIVING
ORGANISMS ARE
CHEMICAL REACTIONS,
AND ENZYMES REGULATE
THE MAJORITY OF THEM.
 ENZYME
Enzymes are biological catalysts.
that are almost invariably proteins. It
catalyzes all parts of metabolism or the
chemical events that take place within a cell.
During the process, the enzyme is not destroyed
and is reused. A cell includes millions of
different enzyme molecules, each in charge of
a different chemical process.
 ENZYME
Enzymes can work in different ways, some
enzymes help break down large molecules into
smaller ones, others build up large molecules
from smaller ones and some enzymes help
change one molecule into another.
STRUCTURES
OF
ENZYMES
 ENZYMES ARE A LINEAR CHAIN OF
AMINO ACIDS, WHICH GIVE RISE TO A
THREE-DIMENSIONAL STRUCTURE.
THE DIFFERENT WAYS IN WHICH AMINO ACIDS
WILL BE ARRANGED IN THE CHAIN WILL
INFLUENCE PROPER PROTEIN FOLDING FOR
THE ENZYME TO BE FUNCTIONALLY ACTIVE.
THE PROTEIN CHAIN FOLDS INTO A
POCKET-LIKE STRUCTURE KNOWN
AS THE ACTIVE SITE.

THE ACTIVE SITE IS A POCKET-

LIKE STRUCTURE THAT HOLDS
THE SUBSTRATE.
 THE SUBSTRATE IS A
SUBSTANCE ACTED UPON
BY AN ENZYME.
HOW DO
ENZYMES
WORK?
 Enzymes work in conjunction with the
substrate. The enzymes and substrates
are always moving and occasionally they
collide at the right speed and orientation
so that the substrate fits into the
enzyme at the active site.
 Enzymes "specialized their active site" to
match the shape of a specific substrate that
they can react with. Once the substrate is
inside the reaction takes place.
The enzyme can either build up or break
down the substrates that specifically bind
to it, and we call the resulting item
“products”.
EXAMPLE:
Function and
Uses of
Enzyme
How Does The
Cell Utilize
Enzymes?
 REACTIONS REQUIRE AN
ENERGY INPUT TO BEGIN; THIS
IS REFERRED TO AS THE
ACTIVATION ENERGY.

ACTIVATION ENERGY IS
REFERRED TO AS THE MINIMUM
AMOUNT OF ENERGY REQUIRED
FOR A REACTION TO TAKE
PLACE.
ORGANISMS CREATED A MECHANISM TO
INCREASE THE RATE OF A CHEMICAL
REACTION. THIS INVOLVES CATALYST, A
CHEMICAL WHICH SPEEDS US REACTION
BUT IS NOT USED UP. IT CAN BE
RECOVERED UNCHANGED AFTER THE
REACTION.
 A CELL PRODUCES A PROTEIN THAT
SERVES AS A CATALYST. AN ENZYME IS A
PROTEIN MOLECULE THAT SPEEDS UP THE
RATE OF A REACTION BY ACTING AS A
CATALYST. ENZYMES ARE FOUND ALL
OVER THE CELL AND CAN BE USED
REPEATEDLY UNTIL THEY WEAR OUT OR
BREAK.
Enzymes Lower Activation Energy
During a chemical reaction,
substrates (A + BC) reach a
transition state (A—B—C) before
they are transformed into
products (AB + C). Compared to
an uncatalyzed reaction (left),
enzymes lower the activation
energy by stabilizing the
transition state into a more
energetically favorable
conformation (right).
Enzymes Speed up Chemical Reaction Rates
Each enzyme has a specific
size and three-dimensional
shape in which it’s specific
to the kind of reactant it
can combine with.
The enzyme binds with the
reactant. The molecule to
which the Enzyme affix
itself (the reactant) is
called known as the
substrate.
Enzymes Speed up Chemical Reaction Rates

When the enzyme binds itself to the substrate

molecule, the new, temporary molecule—the enzyme-
substrate complex —is formed when the substrate is
combined with the enzyme, its chemical bonds are
less stable and more likely to be altered and form
new bonds.
CLASSIFICATION
OF
ENZYMES
 ENZYMES ARE CLASSIFIED INTO
SIX CATEGORIES ACCORDING TO
THE TYPE OF REACTION
CATALYZED:
1. OXIDOREDUCTASES
2. TRANSFERASES
3. HYDROLASES
4. LYASES
5. LIGASES
6. ISOMERASES
 OXIDOREDUCTASES
THESE CATALYZE OXIDATION
AND REDUCTION REACTIONS.
A + B: ⇌
A: + B
E.G. LACTIC ACID FERMENTATION
(LACTATE DEHYDROGENASE)
A + B:
PYRUVATE + NADH
⇌⇌
A: + B
LACTIC ACID +
NAD+
 TRANSFERASES
THESE CATALYZE TRANSFERRING OF A
FUNCTIONAL GROUP FROM ONE MOLECULE
TO ANOTHER.
A + BX ---> AX + B

E.G., PROTEIN TRANSLATION (PEPTIDYL

TRANSFERASES)
 HYDROLASES
THEY CATALYZE THE HYDROLYSIS
OF A BOND. (CATABOLIC)
A + H2O ---> B + C

E.G. PEPSIN HYDROLYZES PEPTIDE

BONDS IN PROTEINS.

LIPASE BREAKS DOWN LIPIDS.

PROTEASE BREAKS DOWN PROTEIN.
 LYASES
THESE CATALYZE THE BREAKAGE OF BONDS
WITHOUT THE USE OF WATER AND OXIDATION
& REDUCTION REACTION.
LYASES GENERATE EITHER A DOUBLE BOND OR
RING TO FUNCTION
A ---> B + C

E.G., ARGININOSUCCINATE LYASE

A ---> B + C
ARGININOSUCCINATE ---> ARGININE +
SUCCINATE
 LIGASES
CATALYZE THE ASSOCIATION OF TWO
MOLECULES.
A + B ---> AB

E.G., DNA LIGASE CATALYZES THE

JOINING OF TWO FRAGMENTS OF DNA
A + B ---> AB
 ISOMERASES
THEY CATALYZE THE FORMATION OF ONE
ISOMER TO ANOTHER.
A ------> B

E.G., PHOSPHOGLUCOSE ISOMERASE

A ------> B
GLUCOSE-6-P ---> FRUCTOSE-6-P
ENZYME HELPERS
 CO-FACTORS AND
CO-ENZYMES
ARE SMALL NON-PROTEIN MOLECULES THAT
ENHANCE THE ENZYME’S FUNCTION
MAY BIND TEMPORARILY OR PERMANENTLY TO
AN ENZYME
USUALLY, HELP TO FORM AN ACTIVE SITE BUT
CAN BIND TO OTHER SECTIONS OF THE
ENZYME TO START OR AID IN A REACTION
THEY MAY BIND LOOSELY TO BOTH ACTIVE
SITES AND SUBSTRATES.
CO-FACTOR AND
CO-ENZYME
 Co-Factors
Are “helper molecules” and are inorganic in nature. Co-factors
participate in Catalysis to help them function properly. These
include metal ions such as zinc, iron, and copper.

Ex.
Fe2+
Zn
K+
 WORKING
MECHANISM OF
A CO-FACTOR
 Without a Co-Factor,
the enzyme will not be
able to bind with the
substrate

Co-Factors can be easily separated from

the protein part of the enzyme, but their
presence is essential for the enzyme
reaction to occur because the enzyme
cannot function without a co-factor.
 Co-Enzyme
ARE ORGANIC CARRIER MOLECULES THAT
HOLD ON TO CERTAIN MOLECULES TO
ENSURE CATALYSIS WILL RUN
SMOOTHLY.

EX.
NADH
NADH⇌ NAD+ + H:
IN LACTATE DEHYDROGENASE
PYRUVATE + NADH ⇌
NAD+
LACTIC ACID +
Environmental Factors
Affecting Enzyme Action
 TEMPERATURE
An optimum activity is reached
at the enzyme's optimum
temperature. If it increases
more it will result in a sharp
decrease in activity as the
enzyme's active site changes
shape. It is now denatured.

The rate of an enzyme-catalyzed

reaction increases as the temperature
increases.
At higher temperatures the rate
decreases
 pH

ENZYMES ARE AFFECTED BY CHANGES IN PH. THE MOST

FAVORABLE PH VALUE - THE POINT WHERE THE ENZYME IS MOST
ACTIVE - IS KNOWN AS THE OPTIMUM PH.

IF THE PH LEVEL IS HIGHER THAN AN ENZYME'S OPTIMUM PH IT

WILL RESULT IN A SHARP DECREASE IN ACTIVITY. AS THE ACTIVE
SITE CHANGES SHAPE. IT IS NOW DENATURED
pH EXTREMELY HIGH OR LOW PH
VALUES GENERALLY RESULT
IN COMPLETE LOSS OF
ACTIVITY FOR MOST
ENZYMES. PH IS ALSO A
FACTOR IN THE STABILITY OF
ENZYMES. AS WITH ACTIVITY,
FOR EACH ENZYME THERE IS
ALSO A REGION OF PH
OPTIMAL STABILITY.
SOME ENZYMES OPERATE
BETTER IN 6-8 PH BUT SOME
OPERATE LOWER THAN THAT.
THE OPTIMUM PH VALUE WILL
VARY GREATLY FROM ONE
ENZYME TO ANOTHER
 Table of Enzymes having
different optimum pH levels:
 SUBSTRATE
CONCENTRATION

If there is enough
substrate available,
enzymes will work best.

As the substrate
concentration rises the
enzyme activity
increases
 SUBSTRATE
CONCENTRATION
When the amount of
accessible substrate
surpasses the number of
enzymes, the substrate
cannot be broken down
any further. The enzyme
concentration is the
reaction's limiting
factor.
 ENZYME
CONCENTRATION
THIS BOOST IN ENZYME
ACTIVITY DOES NOT LAST
INDEFINITELY. WHEN THE
AMOUNT OF ENZYME
ACCESSIBLE SURPASSES
THE AMOUNT OF
SUBSTRATE, NO FURTHER
SUBSTRATE CAN BE
BROKEN DOWN. THE
REACTION IS SLOWED BY
As the concentration of the enzyme THE SUBSTRATE
increases the enzyme activity CONCENTRATION, WHICH
IS THE LIMITING FACTOR.
increases.
key concepts
Activation energy - the minimum energy required for a reaction to occur.

Active site - is the region of an enzyme where substrate molecules bind and
undergo a chemical reaction.

Amino acid - are organic compounds that contain amino and carboxylate
−CO− 2 functional groups, along with a side chain specific to each amino
acid.

Catalysts - a substance that increases the rate of a chemical reaction

without itself undergoing any permanent chemical change.
Chemical reactions - a process that leads to the chemical
transformation of one set of chemical substances to another.

Enzyme - a substance that acts as a catalyst in living organisms,

regulating the rate at which chemical reactions proceed without itself
being altered in the process.

Enzyme-Substrate Complex - is a temporary molecule formed when an

enzyme comes into perfect contact with its substrate.

Metabolism - is the chemical reactions in the body's cells that change

food into energy.
Optimum Activity - is reached at the enzyme's optimum temperature. A continued
increase in temperature results in a sharp decrease in activity as the enzyme's
active site changes shape.

Peptide bond - is a chemical bond formed between two molecules when the
carboxyl group of one molecule reacts with the amino group of the other
molecule.

Products - a product is a substance that is formed as the result of a chemical

reaction.

Protein folding - a process by which a polypeptide chain folds to become a

biologically active protein in its native 3D structure.
Reactant - a substance that enters into and is altered in the
course of a chemical reaction.

Substrate - is a molecule acted upon by an enzyme. A substrate is

loaded into the active site of the enzyme, or the place that allows
weak bonds to be formed between the two molecules.

Transition state - is a particular configuration along the

reaction coordinate. It is defined as the state corresponding to
the highest potential energy along with this reaction coordinate.
 UATION
EVAL
 SOURCES:
Sandeep, D. (2021). CBSE Class 11 - 46. Structure of Enzymes;
Difference between Organic & Inorganic Catalysts (In Hindi) Offered
by [Slides]. Retrieved from https://unacademy.com/lesson/46-
structure-of-enzymes-difference-between-organic-inorganic-
catalysts-in-hindi/ZZM6YZRL
Amoeba Sisters. (2016, August 28). Enzymes (Updated) [Video file].
Retrieved from https://www.youtube.com/watch?
v=qgVFkRn8f10&t=225s
FuseSchool - Global Education. (2017b, July 19). Enzymes | Cells | Biology |
FuseSchool [Video file]. Retrieved from
https://www.youtube.com/watch?v=rlH1ym916Fo
 SOURCES:
Activation Energy and Temperature Dependence | Boundless
Chemistry. (2021). Retrieved November 7, 2021, from
https://courses.lumenlearning.com/boundless-
chemistry/chapter/activation-energy-and-temperature-dependence/
The Biology Project. (n.d.). Energy, Enzymes, and Catalysis Problem
Set. Retrieved November 7, 2021, from
http://www.biology.arizona.edu/biochemistry/problem_sets/energy_e
nzymes_catalysis/01t.html
Enzymes and activation energy. (2021). [PDF]. In Enzymes | Principles
of Biology from Nature Education (Vol. 11, p. 3). Retrieved from
https://dls.ym.edu.tw/course/hb/doc/lecture4-(11)%2011-Enzymes.pdf
SOURCES:
https://courses.lumenlearning.com/boundless-
biology/chapter/enzymes/
Enzymes. (2021, March 22). Retrieved from
https://byjus.com/biology/enzymes/
BioVision, Inc. (n.d.). Coenzymes & Cofactors | Metabolism Assays.
Retrieved November 7, 2021, from
https://www.biovision.com/products/metabolism-assays/coenzymes-
cofactors.html
BBC. (n.d.). Effect of temperature, substrate concentration and pH on
reaction rate - Enzymes - Edexcel - GCSE Biology (Single Science)
Revision - Edexcel. Retrieved November 7, 2021, from
https://www.bbc.co.uk/bitesize/guides/z88hcj6/revision/2