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1. IPAC, MARIEFER P.
Enzyme

3. Objective:
Classify enzymes according to the type of reaction catalyzed and the type
of specificity.
Give examples of the correlation between an enzyme`s common name and
its function.
Describe the effect that enzymes have on the activation energy of a
reaction.
Explain the effect of substrate concentration on enzyme-catalyzed
reaction.
Discuss the role of the active site and the importance of enzyme
specificity.
Describe the difference between the lock-and key model and the induced
fit model of enzyme-substrate complex formation.

4. Type of Protein
Acts as a biological
catalyst
Facilitates and
accelerates chemical
reactions within living
organisms
What is Enzyme?

5. SIX MAIN CATEGORIES OF ENZYMES
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases (synthetases)

6. OXIDOREDUCTASES
The enzyme
Oxidoreductase
catalyzes the oxidation
reaction where the
electrons tend to travel
from one form of a
molecule to the other.

7. TRANSFERASES
The Transferases
enzymes help in the
transportation of the
functional group among
acceptors and donor
molecules.

8. HYDROLASES
Hydrolases are hydrolytic
enzymes, which catalyze the
hydrolysis reaction by adding
water to cleave the bond and
hydrolyze it.

9. LYASES
Adds water, carbon dioxide
or ammonia across double
bonds or eliminate these to
create double bonds.

10. ISOMERASES
The Isomerases enzymes
catalyze the structural
shifts present in a molecule,
thus causing the change in
the shape of the molecule.

11. LIGASES (SYNTHETASES)
The Ligases enzymes are
known to charge the
catalysis of a ligation
process.

12. LACTASE
Common Name: Lactase
Function:
Lactase is an enzyme that catalyzes the hydrolysis of
lactose, a sugar found in milk and dairy products.
The common name "lactase" clearly indicates its role
in lactose digestion.

13. AMYLASE
Common Name: Amylase
Function:
Enzymes that catalyze the hydrolysis of starch
Such as:
Amylose and Amylopectin
into simpler sugars like:
Maltose, Maltotriose, and Dextrins.

14. LIPASE
Common Name: Lipase
Function:
Enzymes that catalyze the hydrolysis of fats and
lipids into:
Glycerol and fatty acids.

15. ACTIVATION ENERGY
Minimum amount of energy that reactant
molecules must possess to undergo a chemical
reaction and transform into products.

16. ENZYME-SUBSTRATE COMPLEX
Binding to specific substrate molecules to
forming an enzyme-substrate complex.
Tailored to interact with particular
substrates.
Enzymes act as
biological
catalysts

17. EFFECTS OF SUBSTRATE CONCENTRATION ON
ENZYME-CATALYZED REACTION
Substrate concentration and
Reaction rate are proportional.
enzyme's active sites become
saturated with substrate
molecules.
Further increases in substrate
concentration do not increase
the reaction rate
Initial Rate of Reaction:
Saturation Effect:
Reaction Saturation:

18. ROLE OF THE ACTIVE SITE AND THE
IMPORTANCE OF ENZYME SPECIFICITY.

19. SUBSTRATE BINDING
Provides a specific three-
dimensional environment.
Often likened to a lock and
key or induced fit model.
Only substrates with the
right shape and chemical
characteristics

20. CATALYSIS
Acceleration of Reactions
Energy Conservation
Specificity
Regulation
Reversible Reactions
Substrate Chanelling
Sensing and Signaling
Several Important Factors:

21. DIFFERENCE OF LOCK & KEY MODEL, AND INDUCED FIT
MODEL

22. LOCK & KEY MODEL
Important Factors to Know:
Lock (Enzyme)
Key (Substrate):
No Change in Active Site
Proposed by Emil Fischer in 1894

23. INDUCED FIT MODEL
Flexibility
Conformational Changes
Specificity
Catalysis
Important Factors to Know:

24. DIFFERENCE OF INDUCED FIT MODEL TO
LOCK AND KEY MODEL
INDUCED FIT
LOCK AND KEY
(The lock) and the substrate (the key)
have rigid, complementary shapes from
the outset.
Both the enzyme and the substrate are
flexible. Active site can change its shape
when the substrate binds to it.
Determined by the pre-existing
complementary shapes of the enzyme
and substrate.
Achieved through both the initial
complementarity of shapes and the
conformational changes induced by
substrate binding.