Chapter 15

Biocatalysis (Part 3)

Chapter review
biocatalysis
Properties and
mechanisms of
actions
Properties Mechanism
of enzymes of enzyme
action
Classification
Activation
energy

Cofactors
Types &
f(x) of
cofactors

Factors
affecting
enzymatic
2 hypotheses reaction

Lock
and key

Models

Induced
fit

Inhibition
reversible

irreversible

Competitive Non
competitive

LEARNING OUTCOMES
Explain the roles and types of inhibitors.
Explain inhibition of enzyme reaction :
- reversible inhibition : competitive and
non competitive inhibitor
- irreversible inhibition : cyanide

What is an inhibitor?
A substance that interacts with the enzyme to
prevent it from working in the normal manner,
hence stopping or slowing a specific
enzymatic reaction.

inhibition
reversible

irreversible

2 types inhibitors

Competitive

Non competitive

- cyanide

INHIBITION
The rate of enzyme-controlled
reactions may be decreased by the
presence of inhibitors. There are two
type of inhibitors:
reversible inhibitors
non reversible inhibitors

Reversible Inhibitors

Inhibitor bind to enzyme by weak bonds

The effect of this type of inhibitor is temporary
Causes no permanent damage to the enzyme

Reversible Inhibitors
The association of the inhibitor and enzyme is
a loose one
It can easily be removed
Removal of the inhibitor restores the activity
of the enzyme to normal
There are two types: competitive inhibitors
and non competitive inhibitors

Reversible Inhibitors
Competitive Inhibitors
It competes with the substrate for the active sites
The inhibitor may have similar structure with
substrate
While it remains bound to the active site, it prevents
other substrate molecules from occupying that site
and so decreases the rate of the reaction

Reversible Inhibitors
Competitive Inhibitors

Reversible Inhibitors
Competitive Inhibitors

The substrate continues to use any unaffected enzyme

Substrate and inhibitor are in direct competition

The greater concentration of substrate, the greater their

chance of finding the active sites more substrate
molecules than inhibitor molecules are around to gain entry
to active site

Reversible Inhibitors
Competitive Inhibitors
If the concentration of the substrate is increased, less
inhibition occurs

Reversible Inhibitors
Competitive Inhibitors

Succinic acid

Succinic
dehydrogenase
Malonic acid

Inhibitor absent The substrate

attaches to the active site of the
enzyme in the normal way.
Reaction takes place as normal.

Inhibitor present The inhibitor

prevents the normal enzymesubstrate complex being formed.
The reaction rate is reduced.

Succinic dehidrogenase (enzyme)

Succinic acid

fumaric acid

Malonic acid (inhibitor)

Reversible Inhibitors

Allosteric
site

Reversible Inhibitors
Non competitive Inhibitors

Not attached to the active site but elsewhere on the

enzyme molecule (allosteric site).

They alter the shape of the enzyme - rendering the active

site unreceptive to substrate OR

Leaving enzyme less effective at catalyzing the conversion

of substrate to product.

Reversible Inhibitors
Non competitive Inhibitors

Reversible Inhibitors
Non competitive Inhibitors

Inhibitors and substrate are not competing for the same

sites

An increase in substrate concentration will not therefore

reduce the effect of the inhibitor.

Allosteric site specific receptor site on some part of the

enzyme molecule remote from the active site.

Reversible Inhibitors
Non competitive Inhibitors
E.g.
i) some poison absorbed from environment act by
inhibiting enzymes
Pesticides DDT and parathion are inhibitor of key
enzymes in nervous system
ii) Many antibiotic are inhibitor of specific enzyme in
bacteria
Penicillin block the active site of enzyme that many
bacteria use to make their cell walls

Reversible Inhibitors
Non competitive Inhibitors

A Competitive inhibitor mimic

the substrate competing for the
active site

A Noncompetitive inhibitor bind to

the enzyme away from the active site,
altering the conformation of the
enzyme so that its active site no
longer function

Inhibition Of enzyme activity

Irreversible Inhibitors

Inhibitors leave the enzyme permanently damaged

Enzyme unable to carry out its catalytic function

Inhibitor attaches to the enzyme by covalent bonds

Irreversible Inhibitors
Heavy metal ions such as mercury (Hg 2+) and silver (Ag
+ ) cause disulphide bonds to break!
These bonds help to maintain the shape of the enzyme
molecule
Once broken the enzyme molecules structure becomes
irreversibly altered with the permanent loss of its
catalytic properties.

Irreversible Inhibitors

Example :
inhibition of cytochrome oxidase complex
by cyanide

Irreversible Inhibitors
Cyanide is a poison chemical compound which can
inhibit the normal activity of cytochrome oxidase
(Cytochrome oxidase is one of a superfamily of proteins which act as the
terminal enzymes of respiratory chains) and enzyme in
mitochondria

 Cyanide bind tightly to the iron atom of the

enzyme cytochrome c oxidase inactivate
the enzyme unable to transport e Blocks the passage of electron transport
chain, STOP the ATP production!

Summary