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Reexamination of aspartoacylase: is this human enzyme really a glycoprotein?
[canavan disease]
Aspartoacylase
catalyzes
the
metabolism
of
an
important
amino
acid
in
the
brain
,
with
the
release
acetate
serving
as
the
source
for
fatty
acid
biosynthesis
.
Defects
in
this
enzyme
lead
to
a
loss
of
activity
and
the
symptoms
of
a
fatal
neurological
disorder
called
Canavan
disease
.
Extensive
evidence
,
including
deglycosylation
studies
,
differential
activity
upon
eukaryotic
host
expression
and
site
directed
mutagenesis
,
have
supported
the
presence
of
a
glycan
that
plays
an
essential
role
in
the
stability
and
catalytic
activity
of
mammalian
aspartoacylase
.
However
,
the
structure
of
this
enzyme
did
not
show
the
presence
of
any
non-amino
acid
components
at
the
putative
glycosylation
site
.
A
more
extensive
study
specifically
designed
to
resolve
this
discrepancy
has
now
shown
that
recombinantly-expressed
human
aspartoacylase
is
not
glycosylated
,
but
is
still
fully
functional
and
stable
even
when
produced
from
a
bacterial
expression
system
.
Alternative
interpretations
of
the
prior
experiments
now
present
a
consistent
picture
of
the
structural
components
of
this
essential
brain
enzyme
.
