Enzymes are protein catalysts that regulate the rate of chemical reactions in living organisms, characterized by their specificity and reliance on substrates. They function under normal conditions, can reverse reactions, and may require cofactors for activity. Enzymes are classified into six major groups based on their functions, and factors such as temperature, pH, and substrate concentration can influence their activity.

1. ENZYMES
They are protein molecules which are in the cell
It plays the role of a catalyst in chemical reactions
What is a catalyst?

2. WHAT IS A CATALYST?
It is called a substance that controls the rate of chemical reactions

3. SO IT IS SAID
In nature, enzymes are specialized proteins that control the rate of chemical reactions
in living organisms.

4. CHARACTERIZE THE ENZYME
Enzymes have a protein structure. The difference between an enzyme and a non-
enzyme is explained in three points.
Enzymes perform their actions under normal conditions, such as maltose, which converts
maltose sugar into glucose at 37 degrees Celsius, but HCL performs this action at a
very high temperature, that is, high temperature is required.
Enzymes can make only a small group of chemical changes, that is, three different
enzymes are needed to break down the three sugars (glucose, lactose, maltose).

5. CONT…
Enzymes have the ability to reverse reactions, but non-enzymatic catalysts do not
have this ability, such as carbonic anhydrase, which has the ability to convert water
and carbon dioxide into hydrocarbonic acid and can convert hydrocarbon back into
water and carbon dioxide.

6. SUBSTRATES?
The material whose speed of reaction is accelerated by enzymes is called Substrate
which remains in the form of products after the reaction

7. THE CHEMICAL NATURE OF ENZYMES
Enzymes are organic catalysts
It is proteinaceous in nature
Formed on the surface of living cells
Has a high molecular weight
A long chain of amino acids joined together by peptide bonds
Some enzymes require compounds called cofactors for their catabolic activity

8. CO FACTOR
For the bibliographic activity of some enzymes, it is very important that the effect of
the cofactor on the enzyme is present and causes the catabolic activity of the enzyme.
Cofactors can be organic compounds or chemical ions such as K, Mg, Ca, Mn, Co, Cu,
Fe, Mo.

9. APO ENZYME + CO FACTOR= HOLO ENZYME
When a cofactor joins an enzyme and forms a common bond, the two are called
holoenzymes
The protein part of Holo enzyme is called Apo enzyme
It is clear here that when the co-factor is combined with the Apo enzyme, then the
Holo enzyme is produced.

10. SPECIFICITY OF ENZYME
All enzymes have specific properties
Each enzyme has the ability to act on a specific substrate
is divided into different groups based on their characteristics

11. ENZYME TYPES ACCORDING TO SPECIFICITY
Absolute Specificity enzyme
Group Specificity enzyme
Linkage or bond Specificity enzyme
Stereo chemical Specificity enzyme

12. ABSOLUTE SPECIFICITY ENZYME
Absolute are specialized enzymes
That is, it can only act on one type of substrate
In this reaction, Lactate Dehyrogenase enzyme acts only on Lactate and changes it to
Pyruvate, whose substrate is Lactate.

13. GROUP SPECIFICITY ENZYME
Such enzymes can act on more than one functional group, such as an amino acid
group, a phosphate group, or a methyl group.
For example, page 30 of the chapter
Like Pepsin, the enzyme acts on any substance containing an amino acid group.

14. LINKAGE OR BOND SPECIFICITY ENZYME
Such enzymes act only on specific chemical bonds, if these chemical bonds are present
in any type of molecule.
That is, the peptidase enzyme acts on the peptide bonds that are in any compound
that these bonds are between amino acids.

15. STEREO CHEMICAL SPECIFICITY ENZYME
This type of enzyme acts only on the steric optical isomer.
Example L Alanine oxidase enzyme
In general, it can be said that each enzyme is a catalyst for a specific activity

16. ASSESSMENT OF THE PAST
Whats the ATP?
ATP is formed as a result of which two important processes?
As a result of which of the following chemical reactions in the cell, AMP is converted to ADP to
ATP?
How much energy is produced when ATP is converted to ADP?
What is the open system?
What is the steady

17. EVALUATION OF PREVIOUS LESSONS?
Enzyme definition?
What is a cofactor?
How many types of enzymes are there according to their specific properties?
What is the function of an enzyme?
Explain the characteristics of enzymes?

18. CLASSIFICATION OF ENZYME
A small number of enzymes such as trypsin, chymotrypsin, and pepsin are traditionally
named by adding a suffix to the end of the substrate, for example, the enzyme that
breaks down collagen is called collagenase, and the enzyme that breaks down lipids
is called lipase. Classified by source or by other institutions
In order to better understand enzymes, enzymes have been divided into six major
groups by the International Biochemical Society (IUB).

19. CLASSIFICATION OF ENZYME
Oxidoreductases:- They are enzymes whose function is oxidation and reduction, i.e.
taking hydrogen electrons from one substance to another.
Transferases:- They are enzymes whose job is to transfer groups from one substance
to another, such as methyl transfer, amino group transfer, etc. Trans aminase, trans
methylase, trans acethylase.
Hydrolases:- They are enzymes that break a molecule at the expense of water, water
is also decomposed and another compound joins the hydrogen of water with one part
and the hydroxyl with the other part. Such as Esterase, Carbohydratease, Nucleuses,
Amidase, Protease.

20. CLASSIFICATION OF ENZYME
Lyases:- They are enzymes that break molecules of a substance without water and
change them into smaller molecules. They are also called C-C bond makers or
destroyers.
Isomerases:- They are enzymes that convert a single molecule into its isomer, such as
converting glucose to fructose.
Ligases/synthetases:- These are the enzymes that combine two molecules to form a
new molecule such as fatty acid synthase, glycogen synthase

21. FUNCTION OF ENZYMES
Speeds up chemical reactions.
These activities are inside the cell or outside the cell.
It is necessary to break down the material in the intestines and stomach
Each enzyme acts on the substrate

22. FACTORS INFLUENCING THE ACTION OF ENZYMES
There are a number of factors that affect enzyme activity
Environmental heat
Ph
Enzyme or substrate concentration
Enzyme and substrate contact with other molecules or substances
Effect of oxidizing agents. Page 166

23. EFFECT OF TEMPERATURE ON ENZYME ACTIVITY

24. EFFECT OF PH ON ENZYME
ph7.4 PH14
0
1
2
3
0
3.5
0 0
‫انزایمونه‬ ‫سیستم‬ ‫دهاضمي‬ ‫رنګ‬ ‫سور‬ ‫کې‬ ‫دیاګرام‬ ‫الندي‬ ‫په‬
‫ښایې‬ ‫را‬ ‫رنګ‬ ‫شین‬، ‫انزایمونه‬ ‫نور‬ ‫بدن‬ ‫د‬
‫انزایمونه‬ ‫سیستم‬ ‫هاضمي‬ ‫د‬ ‫انزایمونه‬ ‫نور‬ ‫دبدن‬

25. EFFECT OF SUBSTRATE CONCENTRATION ON
ENZYME ACTIVITY
If the amount of enzyme is constant
If the substrate concentration starts at a low level
If the concentration of the substrate is gradually increased, the rate of reaction
increases as the substrate increases
Finally, a situation is reached where further addition of substrate does not affect the
reaction rate but decreases

26. ENZYME INHIBITORS
A chemical molecule that inhibits enzyme activity is called a molecule
There are two types of activity
Competitive inhibitors:- These are molecules that bind to the active site of the enzyme
and prevent the binding of the substrate.
Non-competitive: Non-competitive inhibitors are those molecules that do not bind to
the active site or the active site of the enzyme. Prevents connection

27. SUBSTRATE AND ENZYME ADDITION MECHANISM
‫انزایم‬
sub
‫انزایم‬
67%
sub
33%
Enzyme and substrate- complex
or
(lock and key)
‫انزایم‬
67%
sub
33%
Enzyme and substrate- complex
‫انزایم‬
product
Enzyme and product- complex

28. SUBSTRATE AND ENZYME ADDITION MECHANISM
‫انزایم‬
67%
product
33%
+ ‫انزایم‬
‫سبستریټ‬
‫انزایم‬
produ
ct
Enzyme and
product- complex

29. BRIEF DESCRIPTION
In the past, it was thought that each substrate binds to the active part of the enzyme,
which has already been completely assigned to it.
Now it is also believed that each enzyme does not have an active part for the
substrate, but as a result of combining with the substrate, it creates an active part that
is completely ready for the substrate.

30. REGULATION OF ENZYME ACTION
Enzymes self-regulate their actions
Many enzymes control their activity by feedback loops of their product.
Some enzymes exist as proenzymes that are activated when needed, such as
pancreatic enzymes.
Changes in protein structure
by enzyme-inhibiting molecules

31. USING OF ENZYMES
To find the disease
For treatment of disease
To monitor the disease

32. TO FIND THE DISEASE
Different enzymes are used to detect different diseases, some examples are as
follows
The normal level of amylase enzyme is 80-180 units, and this level increases in acute
inflammation of the pancreas.
Alanine transaminase ALT, SGPT enzyme, which is normally 7-56 units in the blood,
increases in inflammatory diseases of the liver.
Aspartate transaminase AST, SGOT are normally 5-40 units in the blood, the amount
increases in acute inflammatory bowel disease, heart attack, and kidney disease.

33. TO FIND THE DISEASE
Lactate dehydrogenase:- lactate dehydrogenase is 140-280 units in normal form, its
amount increases in diseases such as heart attack, kidney disease, kidney cancer.
Lipase lipase is normally 10-160 units or less. Its amount increases in pancreatic
inflammation, pancreatic cancer and other diseases.
Acid phosphatase normally has a level of 1, but is elevated in prostate cancer.
Creatine kinase normally has a value of 60-175 units, its value increases in heart
attacks and muscle diseases.
Cholinesterase cholinesterase is normally 8-18 units URI and increases in heart attack.

34. TO TREAT THE DISEASE
Enzyme is used in the treatment of common problems to deadly diseases.
Digestive system enzymes that are widely available in the market are used for digestion
such as trypsin, chymo trypsin.
Seratio peptidase, an enzyme produced by some bacteria, is used to prevent inflammation.
Streptokinase This enzyme is also made by bacteria and affects the formation of blood
clots inside the veins. It will be used in the treatment of heart attacks or other diseases.
The enzyme called L asparaginase also prevents the combination of the amino acid called
asparagine in the peptide chain, preventing the formation of protein and the growth of
cells. has a role
Thrombin enzyme is also used to prevent bleeding at the site of injury

35. IN DISEASE SURVEILLANCE
In the detection of diseases, we have learned that the level of enzymes in the blood is
constant, if the level increases, it causes disease.
For example, if a person has a bone disease, we follow the level of alkaline
phosphatase enzyme, if it is more than the standard amount, the patient needs to be
treated.