ENZYMES

PART II
- FACTORS AFFECTING
ENZYME ACTION

Explain

the effects of pH, temperature,

enzyme concentration and substrate
concentration on enzyme action

Explain

the effects of competitive and noncompetitive inhibitors on enzyme activity

Investigate

the effects of temperature and

substrate concentration on enzyme activity

OBJECTIVES

As

temperature increases, the kinetic energy

of the enzyme and substrate molecules also
increase

There

is a greater chance of collision

Enzymes

are inactive at low temperatures

Enzyme

activity increases until an optimum

temperature is obtained

TEMPERATURE

 If

the temperature goes beyond the optimum, the

secondary and tertiary structures of the enzymes will
be denatured or destroyed.

Bonding

interactions are disrupted and the active site

Enzyme

activity will be reduced

is lost.

TEMPERATURE

TEMPERATURE

is the optimum temperature

TEMPERATURE

The

change in rate of reaction for each

10C rise in temperature is called the
temperature coeffecient, Q10
Q10 = rate of reaction at (x+10C)
rate of reaction at x

*An example will be given for calculation purposes

TEMPERATURE

 Enzymes

have an optimum pH at which they

work best

Deviations

from the optimum can cause bonds to

be broken (especially hydrogen and ionic bonds),
so the enzyme becomes denatured

These

bonds contribute to the stability of the

tertiary structure of the enzyme

Extremes

in pH change the shape of the enzymes

and their active sites

pH

pH

Given

that all other factors remain

constant, the rate of an enzyme-catalysed
reaction is directly proportional to the
concentration of the enzymes present.

CONCENTRATION OF ENZYMES

As

the substrate concentration increases,

so will the rate of reaction

However,

a point is reached where all the

active sites become filled with substrates
and there is no further increase in rate
(Vmax)

Products

will have to be released from the

active sites for new ES complexes to form

SUBSTRATE CONCENTRATION

SUBSTRATE CONCENTRATION

These

are chemicals which reduce the

rate of an enzyme-catalysed reaction

They

can change the shape of the active

site directly or indirectly

May

be competitive or non-competitive

They

are either reversible or irreversible

INHIBITORS

COMPETITIVE
-

Has a shape
resembling the
normal substrate

Competes with the

substrate to occupy
the active site

INHIBITORS

INHIBITORS

NON

COMPETITIVE
- They do not attach to
the active site
-

Bind with the enzyme

elsewhere but causes
a change in the shape
of the active site

Prevents the formation

of ES complex

INHIBITORS

INHIBITORS

INHIBITORS

INHIBITORS

Antibiotics

called sulphonamides act

as competitive inhibitors

Their shape resembles para-aminobenzoate

(PAB) which harmful bacteria use to make folic
acid, which involves enzyme action

If folic acid is not made, the bacteria will die

EXAMPLES OF INHIBITORS

Heavy

metals like mercury and

arsenic may completely inhibit
enzymes

They combine permanently with

sulphydryl groups

May cause precipitation of the enzyme

molecules

EXAMPLES OF INHIBITORS

The

enzyme succinic dehydrogenase

converts succinate to fumarate in the
Krebs Cycle (involved in respiration)

Malonate fits into the enzymes active site

Competitive inhibition results

EXAMPLES OF INHIBITORS

Acetylcholinesterase

breaks down the

neurotransmitter acetylcholine at the
synapses.

- Organophosphates found in nerve gases

or insecticides inhibit this enzyme in a
non-competitive way

EXAMPLES OF INHIBITION

Pyrethroids

paralyse insects by keeping

the sodium channels open in neuronal
membranes.

Pyrethroids inhibit oxidase enzymes

Organisms cannot metabolise the substance

Lethality persists

EXAMPLES OF INHIBITORS