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Factors Impacting Enzyme Function - Stuart

The document discusses various factors impacting enzyme function, including pH, temperature, enzyme concentration, substrate concentration, and types of inhibition. Each enzyme has specific optimal conditions for activity, and deviations from these conditions can lead to decreased activity or denaturation. Examples such as salivary amylase, Taq polymerase, and malonate illustrate the effects of these factors on enzyme behavior.

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4 views

Factors Impacting Enzyme Function - Stuart

The document discusses various factors impacting enzyme function, including pH, temperature, enzyme concentration, substrate concentration, and types of inhibition. Each enzyme has specific optimal conditions for activity, and deviations from these conditions can lead to decreased activity or denaturation. Examples such as salivary amylase, Taq polymerase, and malonate illustrate the effects of these factors on enzyme behavior.

Uploaded by

stuartsan472
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Factors Impacting

Enzyme Function
pH – shows if a solution is basic or
acidic
• Each enzyme has an optimal pH range where it functions best, with the pH
often being specific to the enzyme’s environment.
• At pH levels which are either too basic or acidic compared to the optimal pH,
the enzyme activity and rate of reaction will decrease as the enzymes
denature in unsuitable pH levels which makes the substrate unable to bind to
the active site as the specific 3D shape of the tertiary structure is no longer
complementary.
• The pH of the environment can influence the binding of substrates to the
active sites of enzymes as the changes in pH can alter the electrostatic
interactions between the enzyme and substrate.
• At extreme pH levels, the loss of enzyme activity may be irreversible while in
a narrow pH range changes to the pH may be reversible and allow the
enzyme to recover its function.
• An example is salivary amylase having an optimal pH range of 6-7 where it
functions and breaks down starch best.
Denaturati Effect of pH on an Enzyme (e.g. salivary
on of amylase)
enzymes

Denaturati
on of
enzymes

acidic basic
Temperature
• All enzymes have an optimal temperature range, where different enzymes function
best at different optimal temperatures.
• The optimal temperature is usually specific to the enzyme’s environment.
• Enzyme activity, and the rate of reaction, is reduced at lower temperatures as the
molecules have less kinetic energy to move around and react.
• The enzyme action and rate of reaction increases when temperature increases up to
the optimum temperature, as there is increased kinetic energy assisting the
substrates to bind to the active sites.
• When the temperature is higher than the optimum temperature the enzyme activity
sharply decreases as they become denatured, where the enzyme’s tertiary structure
is disrupted through breaking of hydrogen bonds and the active sites are not able to
bind to the substrates, therefore decreasing the rate of reaction.
• An example is Taq polymerase which functions optimally at high temperatures
around 72 degrees Celsius and is used in polymerase chain reaction to amplify a
sample of DNA.
The Rate of An Enzyme Catalysed Reaction at Different
Temperatures
This is different for each
enzyme and is usually
specific to the enzyme’s
environment.

()
Enzyme Concentration
• The enzyme activity is directly proportional to the enzyme
concentration if there is an unlimited supply of substrate.
• At higher enzyme concentrations, the rate of reaction will be faster,
at lower enzyme concentrations, the rate of reaction will be slower.
• With a limited amount of substrate, when the enzyme
concentration is increased to a level of enzyme saturation, the
enzyme activity will plateau as all of the active sites will be
saturated with substrate with the excess substrate unable to bind
until the bound substrates are released.
• An example of this is catalase which breaks down hydrogen
peroxide to water and oxygen with an increasing reaction rate until
the enzymes become saturated.
Rate of Reaction with Increasing Enzyme Rate of Reaction with Increasing Enzyme
Concentration and Unlimited Substrate Concentration and Limited Substrate

Does not plateau as


there is an unlimited
amount of substrate Plateaus as there is a
limited amount of
Substrate concentration
• The enzyme activity, rate of reaction, is increased as the substrate
concentration is increased because more substrates are capable of
binding to the active sites of enzymes.
• This continues until a point of enzyme saturation at a specific enzyme
concentration with every enzyme bound to a substrate and where
there is the maximum rate of reaction.
• When the amount of substrate is increased after this, the rate of
reaction does not increase as the substrates can not bind to the active
sites, therefore there is a plateau in the rate of reaction at the point of
enzyme saturation.
• An example is RuBisCO which catalyses the formation of 3-
phosphoglycerate by combining carbon dioxide and RuBP and the rate
of reaction increases with a higher RuBP concentration.
The maximum rate of
reaction that the enzyme
can achieve

The substrate concentration


where the enzyme achieves
half of the Vmax.
An inverse measure of the
affinity of the enzyme and its
substrate.
Competitive Inhibition
• When an inhibitor binds to the active site of an enzyme, this blocks
the substrate to bind to the active site and reduces enzyme activity
and the rate of reaction.
• When there are more inhibitors competing with substrates to bind to
the active sites, there is less enzyme activity and a decreased rate of
reaction.
• However, these competitive inhibitors reversibly and non-covalently
bind to the active sites of the enzyme, which allows them to release
the enzyme so that the substrate can bind to the enzyme when the
substrate concentration is increased.
• An example of a competitive inhibitor is malonate which inhibits
succinate dehydrogenase, by binding to the active site and
preventing succinase from binding.
Non-competitive Inhibition
• The non-competitive inhibitor binds to the allosteric site of the enzyme
which causes the active site to change shape so that it is no longer
complementary to the specific substrate.
• Since the substrate cannot fit into the active site, the enzyme activity
and rate of reaction is decreased.
• There are reversible non-competitive inhibitors which are non-covalently
bound to the allosteric site but can release from the enzyme and allow
the enzyme to function normally.
• There are also irreversible non-competitive inhibitors which covalently
bind to the enzyme and leads to the enzyme being permanently
inactivated leading to reduced enzyme activity.
• Cyanide can bind to the allosteric site of cytochrome c oxidase which
changes the shape of the enzyme and does not allow oxygen to bind.

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