Kurdistan Regional Government – Iraq

Ministry of Higher Education & Scientific Research

University of Duhok
College of health sciences
Department of Medical laboratory sciences

Lect. 2
Enzymology
Biochemistry Theory Lecture

Barhav Issa Abdullah

Asst. Lect. In Biochemistry
Enzymes are made Up of:
1.Fats
2.Proteins
3.Nucleic acids
4.Vitamins
Enzyme catalyzing rearrangement of atomic grouping without altering molecular
weight or number of atom is:
1. Ligase
2. Isomerase
3. Oxidoreductase
4. Hydrolase
• This statement about enzymes is true:
1.Enzymes accelerate reactions by lowering the activation energy
2.Enzymes are proteins whose three-dimensional form is key to their function
3.Enzymes do not alter the overall change in free energy for a reaction
4.All of these

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

 • Which of the following is produced with the combination of
apoenzyme and coenzyme:

1.Holoenzyme
2.Enzyme substrate complex
3.Prosthetic group
4.Enzyme product complex

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

 Some factors affecting enzymatic reactions
1: Concentration of Enzyme
Higher enzyme concentration indicates
that more enzyme molecules are
available to process the substrate. The
high levels of enzyme-substrate
complex result in a higher initial
catalytic rate, which gives the reaction
a HeadStart in the shift toward
reactant-product equilibrium.

(As the concentration of the enzyme is increased, the velocity of the reaction proportionately increases )

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

2: Concentration of Substrate
In the presence of a given amount of enzyme, the rate of enzymatic
reaction increases as the substrate concentration increases until a
limiting rate is reached.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

3: Effect of Temperature
Enzyme- catalyzed reactions are accelerated by increasing the temp
until an optimum value is reached;

at high temperatures the rate decreases again because the enzyme becomes
denatured and can no longer function.
11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)
4: Effect of pH
Enzymes are protein substances that contain acidic carboxylic groups
(COOH–) and basic amino groups (NH2). So, the enzymes are affected
by changing the pH value.
• Some enzymes act best in alkaline medium , other in acid medium
• For every enzyme there is a PH where it acts at its best and this is its
optimal PH.
• But for most biological enzymes the optimum PH is around 7.4.
For example:
• Optimal PH for pepsin → around 2.0
• Optimal PH for trypsin → varies from PH 8.0 – 9.0

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)
11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)
5: Effect of Activators
Some of the enzymes require certain inorganic metallic cations, like
Mg2+, Zn2+, etc., for their optimum activity

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

6. Effect of radiation
At higher radiation doses a marked decrease in the activities of all the
enzymes was observed.
Exposure enzymes to UV, beta, gamma and X-rays inactivate several enzymes
due to formation of peroxidase.
e.g. UV rays inhibits salivary amylase activity.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

 Enzyme Inhibition
• Enzyme inhibitors are molecules that reduce the catalytic activity of
enzymes.
• Reducing of effective enzymatic activity or complete blocking of
enzyme may cause either complete death of cell either modifications
in the pathways.
• Drugs with cause complete inactivation of enzymes from essential
pathways will cause cell death and therefore such drugs can be used
as an antibiotics

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

There are three types of enzyme inhibition reactions :
1. Competitive Inhibition
2. Non-competitive Inhibition
3. Uncompetitive Inhibition

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

1. Competitive Inhibition
A molecule other than the substrate binds to the enzyme’s active site,
causing competitive inhibition. The inhibitor (molecule) has a structural and
chemical similarity to the substrate (hence able to bind to the active site).
The competitive inhibitor hinders substrate binding by blocking the active
site. Since the inhibitor competes with the substrate, increasing the
substrate concentration reduces the inhibitor’s actions

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

2. Non-Competitive Inhibition
A chemical binds to a location other than the active site in non-
competitive inhibition (an allosteric site). When the inhibitor binds to
the allosteric site, the enzyme’s active site undergoes a structural shift.
The active site and substrate no longer share affinity as a result of this
alteration, preventing the substrate from binding. Increased substrate
levels will not be able to reverse the inhibitor’s action since the
inhibitor is not in direct competition with the substrate.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)
3. Uncompetitive Inhibition
The inhibitor binds only to the substrate-enzyme complex in uncompetitive
inhibition. In reactions involving two or more substrates or products,
uncompetitive inhibition is common. Non-competitive inhibition can occur
with or without the presence of the substrate, whereas uncompetitive
inhibition requires the formation of an enzyme substrate complex.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

Clinical Significance of enzyme estimation
• Single or serial assay of serum activity of a selected enzyme
1. Helps in making the diagnosis/differential diagnosis/ early detection
of a disease
2. Helps and find out prognosis of a disease.
3. Helps to detect the response to drugs in a disease.
4. Also help to find out the time course of disease.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

Enzymes as diagnostic markers in different diseases

• Enzyme estimations are helpful in the diagnosis of :

1 Myocardial Infarction
2.Liver diseases
3. Muscle diseases
4.Bone diseases
5.Cancers
6.GI Tract diseases

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

Enzyme-Deficiency Disorders
• Since enzymes are essential to the organism’s biochemical reactions,
deficiencies or abnormalities in the function of an enzyme will have a
direct impact on the organism’s metabolism, resulting in metabolic
syndromes or disorders.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

The following are examples of metabolic disorders that arise from the
abnormalities in the enzyme function:
1. Glucose-6-Phosphate Dehydrogenase (G6PD) Deficiency
G6PD deficiency is also known as "favism," since G6PD deficient
individuals are also sometimes allergic to fava beans. G6PD deficiency
is an allelic abnormality which is inherited in an X-linked recessive
fashion. When someone has G6PD; hemolytic anemia and prolonged
neonatal jaundice are the two major pathologies associated with G6PD
deficiency.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)

2. Gaucher Disease
Gaucher disease is a rare genetic
disease caused by mutations in the
GDA1 gene, leading to the reduction in
the activity of glucocerebrosidase,
Patients suffering from Gaucher
disease are unable to degrade
glucosylceramides and other
glycolipids, and they are instead
deposited in various organs.

11/3/2023 Barhav Issa Abdullah (BIOCHEMIST)