STAGE 2

SACE
BIOLOGY
TOPIC 1: DNA and Proteins
Chapter 1.4
Chapter 1.4: Enzymes

Learning outcomes:
 Describe the induced-fit model of enzyme-substrate binding
 Describe the factors that affects the functions of enzymes
 Enzyme-substrate binding

• Enzyme – globular protein, speeds up/catalyses specific chemical reactions in cells

• Enzyme is also known as …………… - speeding up the rate of reaction without any other
changes.
• Enzymes which is produced and catalyses reactions within cells - ……………………….
• Enzymes which are produced by cells, act outside cells -
………………………………………….
• During enzyme-catalysed reactions, reactants/substrates are converted into ………………..
• This involves breaking of chemical bonds in the substrate and formation of new bonds in the
product.
• Enzymes are not used up in the reaction
Enzyme-substrate binding

• After product is formed, enzyme is released and can be used as

many times.
• The region where substrate bind is called ………………….
• The shape of this region is highly specific.
• The shape of the enzyme and its substrate are said to be
……………………………………….
Enzyme-substrate binding

• In order for any two molecules to react, they need to collide with
sufficient energy and this is possible with the help of enzyme
• Enzyme-substrate binding brings substrate into orientation that
facilitates the breaking and formation of chemical bonds.
• Bonds in substrate are put under stress which lowers the amount of
energy needed to break them and therefore the amount of energy
needed for the reaction to proceed.
Enzyme specificity

• Enzymes are specific for their substrate

• Complementary binding of one specific substrate to the active site
of one type of enzyme is known as …………………
• Enzyme-substrate binding is reversible.
• Some enzymes may convert more than 100 000 substrate molecules
into products per second
 Metabolism and Metabolic pathways

• All biochemical reactions carried out by living organism is called …………………………

• The overall rate of these reactions are called ………………………….
• The separate biochemical reactions that make up a cell’s metabolism are called …………………………………..
• Biochemical processes that are driven by metabolic reactions are called
………………………………………….i.e: respiration and photosynthesis
• Not many chemical reactions in cells occur as a single reaction or one step.
• Most reactions form part of a ………………………………...that consists of chains and cycles of many separate
enzyme-catalysed reactions or many steps.
• Each step in the metabolic pathway is catalysed by specific enzyme.
 Metabolism and Metabolic pathways

• All biochemical reactions carried out by living organism is called …………………………

• The overall rate of these reactions are called ………………………….
• The separate biochemical reactions that make up a cell’s metabolism are called …………………………………..
• Biochemical processes that are driven by metabolic reactions are called
………………………………………….i.e: respiration and photosynthesis
• Not many chemical reactions in cells occur as a single reaction or one step.
• Most reactions form part of a ………………………………...that consists of chains and cycles of many separate
enzyme-catalysed reactions or many steps.
• Each step in the metabolic pathway is catalysed by specific enzyme.
The Induced-fit model

• The active site of enzyme is a groove or cleft on the surface of the

enzyme into which the substrate(s) can bind
• The specificity of the enzyme and substrate is thus explained by the
complementary binding and is this interaction that forms the basks
of how enzymes work.
• The substrate binds to the enzyme by weak bonds which often cause
changes to the shape of both the enzyme and the substrate.
The Induced-fit model

• The original model put forward to explain enzyme action was the
‘lock and key’ model.
• This suggested that the enzyme had an active site which was like the
keyhole for the substrate.
• Specificity was thus explained like a key and lock, only the correct
key can fit into and work in the lock.
The Induced-fit model

• The induced-fit model proposed in the 1950s extends and builds on

this original hypothesis.
• This model does not have the key and lock being a perfect fit but
instead binding together and modifying each others shape in the
process
Watch the video in the links

• All about enzymes -

https://essentialseducation.com.au/online-resources/ecv-enzymes/
• Enzymes -
https://essentialseducation.com.au/online-resources/eva-enzymes/
Lowering activation energy

• Chemical reactions involve breaking of chemical bonds in the molecules

of reactants and the formation of new chemical bonds that hold atoms
together in the products.
• All reactant molecules require energy for their bonds to break and the
energy needed to do this is known as ………………………………….
• The lower the activation energy is, the more quickly a reaction occurs
because less energy is needed to break reactant bonds to initiate the
reaction
 Factors influencing enzyme activity

• One indicator of enzyme activity is the rate at which reactant is converted into product,
or the rate of enzyme-catalysed reaction
• Enzyme activity can be affected by a variety of factors:
Temperature
pH
Concentration of reactants
Concentration of enzymes
Concentration of products
Presence of inhibitors
Temperature
 Temperature

• At low temperatures, enzyme activity increases rapidly as temperature increases. Because of increased
…………………….., enzyme and substrate molecules will move more and more rapidly, resulting in more
collisions at the active site and therefore greater rate of reaction.
• Enzyme activity reaches a maximum at the optimum temperature.
• Temperature increases above the optimum temperature alter the structure of the active site of enzymes. This
process is called ……………………………… Substrates are unable to bind to the denatured active sites
because they are no longer complementary in structure.
• Following denaturation, enzyme activity rapidly reduces to zero.

Humans – optimum temperature for enzyme activity is about ………………………..

Some bacteria that live in hot springs – much higher optimum temperature and able to function at very high
pH
 pH

• At optimum pH, enzyme activity is at a maximum

• pH changes above or below the optimum pH, denatures enzymes. Substrates are unable
to bind to the denatured active sites.
• Enzyme activity decreases to zero very quickly.
• Enzyme-substrate binding is reduced when changing pH alters the shape of the enzyme
or substrate, causing it to no longer be complementary.
• The optimum pH is not the same for all enzymes: eg the optimum pH of enzymes in
blood is approximately 7, while enzymes in stomach is approx. pH 2 (acidic)
• Chemical buffers in the body help to stabilise pH and thus allow enzymes to catalyse
Concentration of reactants

• At low substrate concentrations, enzyme activity increases rapidly as substrate

concentration increases. This results from more collisions between the enzyme
and the substrate at the active site.
• At higher substrate concentrations, most of the active sites on the enzymes are
occupied by substrate, so increases in substrate concentration causes smaller and
smaller increases in enzyme activity.
• Increases in substrate concentration above the optimum substrate concentration do
not lead to greater enzyme activity because all the active sites are occupied by the
substrate.
Concentration of the enzyme

• The rate of an enzyme controlled reaction is also affected by the

concentration of the enzyme
• As the concentration of an enzyme is increased, so does the reaction
rate as there is ample of substrates to bind with the active sites of an
enzyme
• When the substrate concentration becomes a limiting factor, the
addition of more enzyme will not increase the rate of reaction.
Concentration of products

• The activity of some enzymes is regulated by substances which bind to the

enzyme, not at the active site but to a region away from this area.
• This binding can cause a reversible change in the shape of the active site and
as a consequence alter the enzyme-substrate binding.
• End products of metabolic pathways can act in this manner and may act as an
inhibitor of the pathway
• This action is associated with the control of metabolic pathways in cells and
is referred to as ……………………………………………
• End-product inhibition occurs where the presence of a high
concentration of an end-product of a metabolic pathway
inhibits the production of one of the products that in turn stops
the production of the end product
Inhibitors

• A number of molecules exist which can reduce the rate of enzyme-

catalysed reactions that may lead to accumulation of the substrate.
• These molecules are called …………………..
• Two types:
• ………………………………..
• ……………………………….
Competitive inhibitors

• Molecules mimic or have a structure similar to the structure of the

substrate,
• They will compete with substrate by binding to the active site of the
enzymes.
• As a result, enzyme-substrate binding is reduced causing enzyme
activity to decrease.
Non-competitive inhibitors

• These molecules do not compete with the substrate but instead bind
elsewhere on the enzyme at a site which is not active site
• As a result of binding, the structure of shape of the active site changes.
• This also prevents the binding of enzyme and substrate at the active
and thus a reduction in enzyme activity.
• This action underpins the control mechanism for metabolic reactions
in cells termed end-product inhibition
An agricultural application

• Understanding of enzyme inhibitors has led to their use in

agriculture.
• One example of this has been the development and use of herbicides
or chemicals designed to kill weeds.
• Herbicides are used to reduce competition with crops so as to
maintained crop yields and thus profits.
An agricultural application

• Widely used agriculture herbicides is glyphosate which is sold as a

product typically called Roundup or Zero
• When sprayed onto the leaves of weeds, glyphosate quickly passes into
the sugar-transporting tissue@phloem through which is it transported to
all growing part of the weeds.
• Thereafter glyphosate enters the cytosol of plant cells where it acts as
competitive inhibitor of an enzyme that catalyses one step in a metabolic
pathway called the shikimic acid pathway”
 An agricultural application

• This pathway begins with shikimic acid and consists of 7 steps all of which contribute
to the synthesis of products that plants need to grow; without them they quickly die
• One product is an amino acid called phenylalanine which is essential for the synthesis
of specific plant-grown proteins
• Plant cells also need phenylalanine to make a substance called lignin which is needed
to form new cell walls during mitotic division of plant cells.
• Lignin also provide support for plant tissues, especially in the leaves and the stem and
strengthening the water-transporting tissue@xylem to allow plants to transport
materials efficiently from the soil to the leaves.
End-chapter Exercises (powerpoint)

1. What is the role of enzymes in biological systems?

2. How do enzymes reduce the activation energy of a reaction?
3. Distinguish between intracellular and extracellular enzymes
4. a. Define the term active site
b. Where is the active site found?
c. What is a substrate?
d. What is meant by complementary shape as applied to the active site of an enzyme
e. Explain why a different enzyme is required for each step in a biochemical pathway
End-chapter Exercises (powerpoint)

5. Describe the induced-fit model of enzyme-substrate binding.

Include diagram
6. a. State three environmental factors that affect activity of an enzyme
b. Explain how each of these environmental factors affects enzyme
activity
Chapter 1.4 Homework

Complete the homework worksheet attached in CN.

Dateline: One-week