THE SCRIPPS RESEARCH INSTITUTE
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EI,IBARGOEDBY SCIENCE FOR!
Broadcast ltediar 3 P.p. (Pacific
Time),
Print
l,ledia, Friday,
June 5, 1992
Thursday,
ilune 4, 1992
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Manager
I{IRROR-II{,AGE WORLD OF BIOLOGICAL UOLECUI,ES
EXPI.OREDBY SCRIPPS RESEARCHERS
Unique
Enzfme Prepared by Total
Chemical
First
Glinpse of Looking-Glass
LA JoLr"A,
cALrF.
scientists
have
occurring
enzyme.
The work
headed
by
is
The research
B.H.
in
Kent,
La Jo1la,
is the first
Kent
the simplest
microorganism
they've
forces
dictated
notes
scientists
wondered
mirror-image
known
if
structures
to
the
L99z
rrmirror-imaqerr
exist
a particular
that
ph.D.,
Reveals
For the
announeed in the June 5 issue
catalysts.
left-handed.
June 4,
synthesized
stephen
(TSRI)
Institute
3 p.m.
Synthesis
World
from
f irst
of
a
tirne,
naturalllr-
of
Science
by a team
The
scripps
Research
California.
example of ttright-handedtt
throughout
life
to mammals, all
planet,
on this
biological
catalysts
have long wondered why this
mirror-image
enzyme
r oE whether
in
the
handedness
at
in
UORE
the
biorogical
are
And,
would
have
the
sub-atomic
from
was so.
molecules
and properties
nature
biological
aslrmmetric
level
universe.
also
PAGA 2 --
RESEARCE INSTITUTE
TEE SCRIPPS
indicates
The TSRI research
of
properties
rrwe've
irnplies
forms
now shown that
evolved
just
work
would
in
and
interactions
world
sure.
opposite
the
life
Science
article
This
mirror-image
could
and that
actually
mirror
nobody knew for
made up of
as weti,
the
inside
equally
have
way. tt
that
of
authors
Additional
del,.
Raymond c.
chemists
the
systems
living
that
in
except
rrBefore this,
Kent remarked.
existsrrr
structures
rnirror-image
molecules.
asymmetrical
other
have
pair
and right-handed
a left-
indistinguishable
are
which
involving
enzymes
identical
otherwise
that
the
Milton,
Saskia
and
Ph.D.
TSRI protein
are
C.F.
Milton,
Ph. D.
note
The researchers
large
amino acids)
are
team
called
Enzymes
act
Without
change.
These
biological
shape
at
formed
long
and is
the
right-handedness,
in
the
flexible
cells
life
natural
is
called
as
as
level.
IIORE
called
enzymes
amino
TSRI
naturally-
the viabifity
of
designation
rDrr for
D-HIV protease.
we know
to
it
properties
The shape of
amino acids.
very
by the
the
for
crucial
catalysts
process
--
left-handed
of
mirror-image
owe their
understood
of
made up of
scientific
enzyme is
catalysts
chain
the
the
enzyrnes,
a poorly
AII
nature.
an enzyme that
inside
molecular
in
blocks
of building
The ned enzyrne synthesized
Using
AIDS virus.
the
chains
and are
acids.
L-amino
HIV protease,
occurring
of
rrleft-handedtr
rrright-handedrr
is
long
are proteins
(which
enzymes
asymmetrically
exist
considered
acids
of
comprised
nolecules
that
induce
could
to
chemical
not
their
exist.
precise
an enzlrme molecule
by precise
folding
of
is
the
PAGE 3 --
TEE SCRIPPS RESEARCH INSTITUTE
enzlrme would
the
contain
prove
by
of
the
is
not
that
molecules
the mirror-image
by
the
time
first
be prepared
The new D-enzyme can only
synthesis,
chernical
direct
this
a mirror-image
and activity
structure
to synthesize
supposition.
that
that
suspected
opposite
have been able
researchers
long
version,
naturally-occurring
to
have
scientists
Although
DNA/genetic
recombinant
engineering.
first
in
HIV protease
of the
and
most
of
current
is
synthetic
chemists
of
announced
chemical
this
to
new technique
in
With
obtain
to
Kent
fasteners.
protease
the
more
design
by
is
the
because
of
drug
design
large
molecules.
the
TSRI
build
molecule
with.
In the April
researcher
Martina
amino
the
L
acid
10,
and
L992
Schnolzer
chains
are presently
Miltons
synthesize
organic
largest
large
and the
The HIV
D forms
with
utilizing
of
HIV
the
amounts.
large
both
than
and
Kent
new method
a
very
are used to dealing
Science,
drug
AIDS therapy.
larger
l0-fold
Institute
The HIV protease
the world.
for
form
structure
Cancer
AIDS
in
Kent's
left-handed
its
National
used
D and L enzymes are
the
was
of the molecular
at the
target
potential
for
protease
issue
around
laboratories
implications
determination
information
the
important
Both
the
work
the
to
HIV enzyme in
by researchers
provided
has
hundreds
now
to
led
This
contributed
of the
synthesis
chemical
1988.
that
research
Previous
L and D versions
x-ray
accurate
of
an enzlrme,
crystallographic
researchers
can
data
its
about
structure.
rrThe far
at
better
the
actual
site
Saskia
Milton.
trlt
substrates.
resolution
where
wiII
the
help
The end result
so obtained
wiII
enzyme binds
us deterrnine
should
###
to
allow
substratesrtt
how the
be better
us to
look
added
enzyme works
designed
drugs.tt
on