1. Why
is
it
advantageous
to
have
the
synthesis
and
the
degradation
of
glycogen
controlled
by
different
enzymes?
Because
glycogen
synthetic
and
degradative
pathways
both
occur
in
the
cytoplasm,
having
these
processes
controlled
by
different
enzymes
prevents
a
useless
cycle
of
breaking
down
newly
made
glycogen.
To
prevent
this
futile
cycling,
the
rate
limiting
enzymes
in
each
pathway
are
controlled
allosterically
and
coordinately.
Thus,
allosteric
modulators
that
activate
glycogen
phosphorylase
and
inactivate
glycogen
synthase
allowing
metabolic
flux
to
proceed
in
one
direction.
2. Glycogen
catabolism
releases
glucose-1-phosphate,
the
substrate
used
by
the
first
enzyme
in
the
synthetic
pathway;
what
prevents
a
futile
cycling
of
glucose
into
and
out
of
glycogen?
In
order
for
the
glucose-1-phosphate
to
be
re-made
into
glucogen,
it
must
be
converted
into
UDP-glucose
by
a
reaction
that
is
coupled
to
glycogen
synthase.
If
glycogen
synthase
activity
is
reduced
then
the
necessary
release
and
hydrolysis
of
pyrophosphate
is
also
decreased,
effectively
preventing
the
synthetic
reactions.
3. Which
condition,
a
muscle
phosphorylase
deficiency
or
a
muscle
glycogen
synthase
activity
deficiency,
do
you
think
would
easier
to
treat?
A
glycogen
synthase
deficiency
because
the
glucose
that
enters
muscle
does
not
become
trapped
as
glycogen
and
could
be
used
by
the
tissue
or
dephosphorylated
and
released
back
into
circulation.
Dietary
control
would
be
much
simpler
because
the
issue
is
making
sure
enough
glucose
is
present
in
circulation.
A
phosphorylase
activity
defect
would
allow
gluocse
to
accumulate
in
muscle
and
liver
as
glycogen
without
an
easy
way
to
make
in
available.
4. Allosteric
modulators
act
by
binding
to
the
enzyme
whereas
covalent
modification
(phosphorylation)
is
catalytic
process
which
do
you
think
provides
a
more
rapid
change
in
metabolic
flux?
Covalent
modification,
because
once
an
enzyme
becomes
phosphorylated
(and
activated
for
example)
will
maintain
that
level
of
activity
until
the
phosphate
is
removed.
An
allosteric
modulator
can
easily
diffuse
out
of
its
binding
site
on
the
enzyme,
so
its
activation
of
inhibition
tends
to
be
more
transient.
Furthermore,
changes
to
enzyme
activity
through
phophorylation
are
enzymatic
processes,
so
many
enzymes
can
be
activated
as
a
result
of
a
single
signal.
This
accounts
for
the
rapidity
of
the
process,
one
activated
enzyme
can
produce
hundreds
of
enzymes
producing
thousands
of
products
whereas
one
allowsteric
modulator
can
only
affect
one
enzyme
as
it
produces
its
product.