The action of an enzyme can be controlled by its product (feed back).
Accumulation of the product slows down the rate of chemical reaction.
There is, however, a more complicated system of control in linked systems.
Many reactions in the cell take place in a series of steps, each step being controlled by a separate enzyme.
The substrate S1 gives rise to the product S2 through a reaction controlled by the enzyme E1.
S2 now becomes the substrate of another reaction controlled by the enzyme E2, and so on.
In the synthesis of different amino acids from aspartate, lysine is formed after several steps. Aspartate-->Aspartyl phosphate--> Aspartyl semialdehyde-->Lysine
It has been found that the addition of lysine stops the whole chain of reactions.
Here inhibition is produced not in the last step of the series, but in the first step.
Thus lysine affects the action of an enzyme which is producing an entirely different substance.
This
has
been
explained
by
suggesting
that
the
enzyme
has
a
'control
site'
in
addition
to
the
'active
site'
.
When
the
control
site
is
occupied
by
a
control
substance
(lysine,
in
this
case),
the
latter
distorts
the
shape
of
the
enzyme
One
or
more
reactive
amino
acids
are
removed
from
the
active
site,
which
is
thus
rendered
nonfunctional.
Enzymes
which
undergo
this
type
of
behaviour
are
called
allosteric
enzymes.
They
control
an
entire
series
of
reaction
through
the
end
product.