15.

1 PROPERTIES OF ENZYME AND

MECHANISM OF ACTIONS

15.2 COFACTORS

15.3 INHIBITION

15.0
BIOCATALYSIS

15.2 Explain the types and functions of cofactors
Learning Outcomes
1. A non protein components essential for some enzyme
to function efficiently.
2. Enzyme which bound to a cofactor is holoenzyme.
3. Enzyme without a cofactor is called apoenzyme.
4. More stable than enzyme under high temperature.
5. May be bound tightly to the active site as permanent
residents.
6. Or they may bind loosely and reversibly along with
the substrate.
Cofactors
Learning Outcomes:
15.2 Explain the types and functions of cofactors

ENZYMES
Protein Conjugated protein
Protein Non-protein
Apoenzyme Cofactors
Inorganic Organic
Bind loosely Bind tightly
Metal ions
Prosthetic group Coenzyme
Learning Outcomes:
15.2 Explain the types and functions of cofactors

Metal Ions
1. Inorganic substances, usually loosely bound to the
enzyme which allow an enzyme substrate complex
to form easily.
2. Mostly trace elements that are needed in very
small amounts.
3. Eg: Ca
2+
(in thrombokinase), Mg
2+
4. Others: Ferum, Cobalt, Copper, Zinc
5. Few are inorganic ions.
6. Eg: Chloride ions (in salivary amylase)
Learning Outcomes:
15.2 Explain the types and functions of cofactors

Coenzymes
1. Organic compound, that are loosely bound
with enzymes.
2. Most coenzymes are derived from vitamins
especially group B vitamins
3. Eg: NAD
+
, NADP
+
, coenzyme A, ATP
Learning Outcomes:
15.2 Explain the types and functions of cofactors

Coenzymes
Vitamin Coenzyme
Niacin NAD
+
Pantothenic
acid
Coenzyme A
(CoA)
Vitamin B12 Coenzyme B12
Learning Outcomes:
15.2 Explain the types and functions of cofactors

Prosthetic Groups
1. Organic compound that tightly bound to the
enzymes.
2. Always present and considered permanently
bound.
3. Eg: haem (prosthetic group of catalase in
liver).
4. Others: FAD, FMN, biot,cytochrome.
Learning Outcomes:
15.2 Explain the types and functions of cofactors




Structure of FAD
nitrogens 1 & 5 carry hydrogens in FADH
2

Learning Outcomes:
15.2 Explain the types and functions of cofactors

Action of an enzyme cofactor
Learning Outcomes:
14.2 Explain the types and functions of cofactors

Metal ions as cofactors
Learning Outcomes:
14.2 Explain the types and functions of cofactors

15.1 PROPERTIES OF ENZYME AND
MECHANISM OF ACTIONS

15.2 COFACTORS

15.3 INHIBITION

15.0
BIOCATALYSIS

15.3 Explain the roles and type of
inhibitors
a) Explain reversible inhibition :
competitive and non competitive
inhibitors
b) Explain irreversible inhibition
Learning Outcomes
Inhibitor
Definition
A substance that reduce the rate of enzyme
reaction.

Inhibitor combines with the enzyme to form an
enzyme-inhibitor complex (EI complex).

It prevents the substrate to bind with the
enzyme to form ES complex.

The rate of reaction decrease.
Learning Outcomes:
15.3 Explain the roles and type of inhibitors
Groups of Inhibitors
Inhibitors
Reversible Irreversible
Competitive Non-competitive
Learning Outcomes:
15.3 Explain the roles and type of inhibitors
15.3 Explain the roles and type of
inhibitors
a) Explain reversible inhibition :
competitive and non competitive
inhibitors
b) Explain irreversible inhibition
Learning Outcomes
Reversible Inhibition
- The effect of this type of inhibitor is temporary.
- The inhibitor forms weak bonds with the enzyme.
- It binds loosely, so it can easily be removed.
- When reversible inhibitors are removed, the activity
of the enzyme returns to normal, causes no
permanent damage to the enzyme.
- There are 2 types of inhibitors:
Competitive inhibitors
Non-competitive inhibitors
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Competitive Inhibitors
1. Competitive inhibitors have similar structure with
the substrate.
2. It can fits into the active site of enzyme.
3. It competes with the substrate to bind to the active
sites of enzyme.
4. When it binds to the active site, it produces
enzyme-inhibitor complex (EI complex)
5. As it binds, it prevents the substrate from binding
with the active site.
6. EI complex cannot form the desired products.
7. Thus, the rate of reaction is reduced.
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Overview
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Competitive inhibitor
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


8. However, substrates can still bind with the
unaffected active sites.
9. The same quantity of product is formed at the end
of reaction, but it takes longer time than usual.
10. By increasing the concentration of substrates,
substrates will have more chance to bind with the
active sites compared to competitive inhibitors.
11. The effect of competitive inhibitors can be
overcome.
12. The activity of enzyme is restored to normal when
the inhibitors is removed.
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Competitive Inhibitors
Example:
1. Enzyme : succinate
dehydrogenase
2. Substrate : succinate
3. Product : fumarate
4. Competitive inhibitor : malonate

Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


1. Non-competitive inhibitors have different structure
with the substrate.
2. It does not compete with the substrate to bind to the
active sites of enzyme.
3. Because it binds to other site called allosteric site.
4. When it binds to the allosteric site, it changes the
conformation of enzyme.
5. The shape of active site is altered.
6. Substrate cannot bind to the active site as long as
non-competitive inhibitors binds to the allosteric
site.
Non-Competitive Inhibitors
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


8. The activity of enzyme is restored to normal
when the inhibitor is removed.
9. As the inhibitors do not compete for the same
active site with the substrate, increasing the
substrate concentration will not increase the
rate of reaction.
10. Therefore, the effect of non-competitive
inhibitors could not be reduced.
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Non- Competitive inhibitor
Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


Learning Outcomes:
15.3 a) Explain reversible inhibition :competitive and non competitive inhibitors


15.3 Explain the roles and type of
inhibitors
a) Explain reversible inhibition :
competitive and non competitive
inhibitors
b) Explain irreversible inhibition
Learning Outcomes
Irreversible Inhibitors
1. The effect of this type of inhibitor is permanent.

2. Inhibitors bind tightly by covalent bond or strong
non-covalent bond to the enzyme.

3. So, it cant easily be removed & bind permanently.

4. Causes a permanent damage to the enzyme.

5. Eg: cyanide, CO, paraquat (herbicide),
insecticides, nerve gas.
Learning Outcomes:
15.3 b) Explain irreversible inhibition

Cyanide
1. Cyanide is a deadly chemical found in form of gas,
liquid or crystal form.
2. It has a bitter almond smell.
3. Contained in cigarette smoke, used in industries eg:
plastic and paper.
4. Cyanide will bind with (iron) in cytochrome oxidase.
5. Block the passage of electron through the chain.
6. Permanently inhibits ATP synthesis during cell
respiration.
7. Cytochrome oxidase cannot pass electron to
oxygen.

Learning Outcomes:
15.3 b) Explain irreversible inhibition