Please enable JavaScript.
Coggle requires JavaScript to display documents.
Factors Affecting Enzymes Activity - Coggle Diagram
Factors Affecting
Enzymes Activity
Substrate
Concentration
the availability of substrate
affects rate of reaction
when conc of
ENZYME
kept at
fixed rate...
INITIALLY
level of substrate
increase
level of enzyme activity
increase
more substrates to fill
active sites
more ES complexes
more broken down/built up
AT A CERTAIN POINT
rate levels off
no. enzyme active
limiting
available enzymes working
at max rate
so addition more substrate
no increased effect
Enzyme
Concentration
when conc of
SUBSTRATE
kept
at a fixed rate...
INITIALLY
level of enzyme
increases
level of enzyme activity
increases
more active sites = more
ES complexes
more broken down/built up
AFTER A CERTAIN POINT
rate levels off
no. substrates become
limiting
all available substrates
in active sites already
so addition more enzymes
no increased effect
However, most enzyme-catalysed
reactions - substrate conc
SELDOM
LIMITING
... usually enough substrate allow rate
to increase to max
many adaptions to
ensure that no enzymes
larger than substrates
extensive infolding mitochondrial
cristae to increase SA
no. respiratory enzymes located
on membrane
Temperature
UP TO OPTIMUM
temp increases
rate if enzyme activity
increase
both sub + enz more kinetic
energy
molecules move faster
increasing possibility collisions
increasing ES-complexes
normally activity
doubles every 10°C
ABOVE OPTIMUM
increasing temp breaks
hydrogen bonds
as rises more, more bonds
break + shape active site changes
denatured - permanent + irreversible
enzyme ceases function
Optimum
Temperature
varies in different
living organisms
bacteria inhabit hot
springs - opt = 80°C
species that cannot
control internal temp =
opt for enzymes closely
mirrors temp environment
mammals = 40°C
plants = well below
mammals
pH
either side of optimum
changes in pH will
reduce activity
when
NOT
optimum...
ionic bonds of tertiary structure
are disrupted
active site shape changes
greater deviation from optimum
the greater the disruption bonds
eventually - denatured