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Biology
Enzymes
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Cards (37)
Enzymes
Biological
catalysts
that
increase
the rate of reactions
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Amylase
Catalyzes the breakdown of
starch
molecules into the disaccharide
maltose
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Substrate
The
molecule
that the enzyme
attaches
to
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Products
The
molecules
that are produced by the
enzyme-catalyzed
reaction
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Enzyme-substrate
complex
When the
substrate
molecule fits perfectly into the
active
site of the enzyme
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Enzyme present
Activation energy barrier
is
lower
than without the enzyme
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Lock and key model
The tertiary structure of the active site is fixed and does not change shape, the
substrate
molecule slots perfectly into the
active
site
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Effective temperature on enzymes
The effect of
temperature
on the rate of
enzyme-controlled
reactions
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Investigating the effect of temperature on enzyme-controlled reactions
1.
Select
an enzyme
2.
Measure
amount of product formed over time
3.
Repeat
at range of temperatures
4. Draw
tangents
to measure rate at each temperature
5. Ensure tangents drawn at
same
time point
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Effect of temperature on enzyme-controlled reactions
Rate
increases
as temperature
increases
up to optimum temperature
Rate
decreases
as temperature
increases
past optimum temperature
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Increasing temperature
Increases
kinetic energy
of enzyme and substrate
Increases frequency of
collisions
between
substrate
and active site
Increases rate of
reaction
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Optimum temperature
Temperature at which reaction rate is
maximum
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Human
enzymes have optimum temperature around
40°C
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Enzymes in organisms like bacteria in hot springs have optimum temperature around
70-80°C
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Effect of temperature above optimum
1. Enzyme molecules
vibrate
more rapidly
2.
Bonds
within enzyme break
3.
Tertiary
structure changes
4. Active site no longer
complementary
to substrate
5. Enzyme
denatures
and no longer
functions
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Denatured
enzymes cannot
renature
if cooled back down
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pH
Measure of the
concentration
of
hydrogen
ions in a solution
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Low
pH
(e.g. pH
2
)
High
concentration of
hydrogen
ions
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High
pH
(e.g. pH 6)
Low
concentration of
hydrogen
ions
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Enzymes
Affected by
pH
Work
fastest
at a specific optimum
pH
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Enzymes with different optimum pH
Salivary amylase
(optimum pH around
7
)
Enzyme in
stomach
(optimum pH around
2
)
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pH changes away from optimum pH
Rate of enzyme reaction
decreases
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How pH affects enzymes
1.
Hydrogen
ions can bond with
R
groups of amino acids in active site
2.
Hydrogen
ions can break bonds holding
tertiary
structure in place
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pH
falls (concentration of
hydrogen
ions rises)
Bonds
between
amino acids
break
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pH rises
(concentration of hydrogen ions falls)
Bonds
between
amino acids
form
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Significant
pH
change
Active site
changes shape so much that it's no longer complementary to substrate,
enzyme denatures
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Steps to calculate pH
1. Enter [
H+
] into calculator
2. Press
log
button
3.
Reverse
sign to get pH
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Frequency of collisions
The number of
collisions
per
second
between the substrate molecules and the active site of the enzyme
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Substrate concentration is
doubled
Frequency of collisions between substrate and active site also
doubles
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Frequency of collisions between
substrate
and
active site doubles
Rate of
reaction
also
doubles
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Rate of an enzyme catalyzed reaction
Directly proportional
to the substrate
concentration
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V max
The
fastest
rate at which the
enzyme
can work
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Enzyme is
saturated
Every
active site
is colliding with a substrate molecule, so increasing substrate concentration further will
not
increase the rate
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Enzyme concentration is
low
, substrate concentration is
high
Rate of reaction is relatively
low
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Enzyme concentration is
doubled
Frequency of collisions between substrate and active sites also
doubles
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Rate of an enzyme catalyzed reaction
Directly proportional to the enzyme
concentration
, provided there is more
substrate
than enzyme
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If the amount of substrate becomes limited, increasing the
enzyme concentration
further will not
increase
the rate
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