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Chapter 5 Bio
Chapter 5 Bio
ENZYMES
By Ms. Stephanie B 1
Learning objectives
5.1 Enzymes
Core
1. Describe a catalyst as a substance that increases the rate of a chemical
reaction and is not changed by the reaction
2. Describe enzymes as proteins that are involved in all metabolic
reactions, where they function as biological catalysts
3. Describe why enzymes are important in all living organisms in terms of a
reaction rate necessary to sustain life
4. Describe enzyme action with reference to the shape of the active site of
an enzyme being complementary to its substrate and the formation of
products
5. Investigate and describe the effect of changes in temperature and pH on
enzyme activity with reference to optimum temperature and denaturation
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Learning objectives
5.1 Enzymes
Supplement
6. Explain enzyme action with reference to: active site, enzyme-substrate
complex, substrate and product
7. Explain the specificity of enzymes in terms of the complementary shape
and fit of the active site with the substrate
8. Explain the effect of changes in temperature on enzyme activity in terms
of kinetic energy, shape and fit, frequency of effective collisions and
denaturation
9. Explain the effect of changes in pH on enzyme activity in terms of shape
and fit and denaturation
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Biological catalysts
Without enzymes, the reactions would take place very slowly, or not at all.
Enzymes ensure that the rates of metabolic reactions are great enough to
sustain life.
Enzymes either :
Key Definition
hydrogen
catalase hydrogen + water
peroxide
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Biological catalysts-The active site
• Active site = the part of an enzyme that a substrate molecule fits into
• Substrate = the substance on which an enzyme acts upon
• Product = the substance which is made by the reaction
Each enzyme
can only act on
a particular kind
of substrate
e.g. amylase
cannot break
down protein
molecules,
because they
do not fit into its
active site
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How enzymes work
Eachtype of enzyme has
molecules with a very specific
shape.
Theenzyme molecule has a
‘dent’ in it, called the active site.
An enzyme works by allowing a
molecule of its substrate to fit into
the active site, where the
substrate and the enzyme bind
together. For this to happen, the
fit has to be perfect.
Theshape of the enzyme and the
shape of the substrate are
complementary to one another. 10
How enzymes work
Whenthe substrate is in the active site and bound to the enzyme, the
enzyme makes the substrate change into a new substance called the
product. Then the product breaks away from the enzyme.
Nowthe enzyme is free, and ready to bind with another substrate
molecule.
The short-lived
structure that forms
as the substrate slots
into the enzyme’s Enzyme-
active site substrate
complex
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Properties of enzymes
1. All enzymes are proteins .
2. Enzymes are made inactive by high temperature .
• Enzymes are protein molecules. Thus, can be damaged by heat.
3. Enzymes work best at a particular temperature.
• Enzymes in the human body work best at 37 ºC .
4. Enzymes work best at a particular pH.
5. Enzymes are catalysts .
• Enzymes are not changed in the reaction
• They can be used over and over again, so a small amount of enzyme
can change a lot of substrate into product.
6. Enzymes are specific .
• Each kind of enzyme will only catalyse one kind of chemical reaction.
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Factors that affect enzyme activity
Temperature pH
* Different enzymes
have different optimum
temperatures*
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Explaining how temperature affects enzyme activity
At 0 °C, the enzyme has no activity.
• At this temperature, molecules have very little
kinetic energy – they are moving only slowly.
• As they are moving only slowly, the substrate
molecules rarely collide with the enzyme. So,
they rarely enter its active site, and very few
substrate molecules are converted to product.
Asthe temperature increases, the kinetic energy of the enzyme and
substrate molecules increases.
• They move faster and collide with each other more frequently and
with more energy. Effective collisions are more frequent.
• More substrate molecules collide with an active site and are converted
to product. 14
Explaining how temperature affects enzyme activity
The temperature at which an enzyme works fastest is called its
optimum temperature .
Astemperature increases above the optimum, the kinetic energy of the
enzyme begins to shake it apart.
• Its molecules begin to lose their shape, so that the active site is no
longer a true complementary shape to the substrate.
• When a substrate molecule collides with an active site, it may not fit.
• It cannot form an enzyme–substrate complex and is not converted to
product. The activity of the enzyme therefore decreases.
• When the temperature increases further, the active site is so out of
shape that the enzyme has completely stopped working. It is
completely denatured . 15
Explaining how temperature affects enzyme activity
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pH and enzyme activity
The pH of a solution affects the shape of an enzyme.
Most enzymes are their correct shape at a pH of about 7 - that is, neutral.
Ifthe pH becomes very acidic or very alkaline, then they are denatured.
• This means that the active site no longer fits the substrate,
• So the enzyme can no longer catalyse its reaction.
Some enzymes have an optimum pH that is not
neutral:
• For example, there is a protease enzyme in
the human stomach that has an optimum pH
of about 2.
• This is because we have hydrochloric acid in
our stomachs. This protease must be able to
work well in these very acidic conditions.
Explaining how pH affects enzyme activity
Eachenzyme molecule has a very specific shape, with the active site
being the best fit for the substrate at its optimum pH.
A pH well above or below the optimum causes the enzyme molecule to
lose its shape (denature), so it can no longer bind with the substrate.
denatured denatured
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Explaining how pH affects enzyme activity
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Let’s answer!
The diagram shows an enzyme and a molecule of its substrate, maltose.
The enzyme is able to split a maltose molecule into two glucose molecules.
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Let’s answer!
• The diagram shows an enzyme and a molecule of its substrate, maltose.
The enzyme is able to split a maltose molecule into two glucose
molecules.
Active site
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