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Rael's comment: Great news ! So soon we will be able to reprogram
our genetic code so our sperm will taste like chocolate... That
should be a good incentive for fellatios... Brigitte I am the
first on the list !
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Source:
http://www.scienced
aily.com/ releases/ 2008/08/08082017 4712.htm
<http://www.scienced
aily.com/ releases/ 2008/08/08082017 4712.htm>
Strawberry-flavored Banana? Biochemists Manipulate Fruit Flavor
Enzymes ScienceDaily (Aug. 20, 2008) =E2=80=94 Would you like a
lemony watermelon? How about a strawberry-flavored banana?
Biochemists at The University of Texas Medical School at Houston
say the day may be coming when scientists will be able to fine
tune enzymes responsible for flavors in fruits and vegetables. In
addition, it could lead to environmentally- friendly pest control.
UT Medical School Assistant Professor C.S. Raman, Ph.D., and his
colleagues have re****ted that they were able to manipulate flavor
enzymes found in a popular plant model, Arabidopsis thaliana, by
genetic means. The enzymes=E2=80=94allene oxide synthase (AOS) and
hydroperoxide lyase (HPL)=E2=80=94produce jasmonate (responsible
for the unique scent of jasmine flowers) and green leaf volatiles
(GLV) respectively. GLVs confer characteristic aromas to fruits
and vegetables. Green leaf volatiles and jasmonates emitted by
plants also serve to ward off predators. "Mind you plants can't
run away from bugs and other pests. They need to deal with them.
One of the things they do is to release volatile substances into
the air so as to attract predators of the bugs," Raman said.
"Genetic engineering/ modification (GM) of green leaf volatile
production holds significant potential towards formulating
environmentally friendly pest-control strategies. It also has
im****tant implications for manipulating food flavor," said Raman,
the senior author. "For example, the aroma of virgin olive oil
stems from the volatiles synthesized by olives. By modifying the
activity of enzymes that generate these substances, it may be
possible to alter the flavor of the resulting oils." According
to Raman, "Our work shows how you can convert one enzyme to
another and, more im****tantly, provides the needed information
for modifying the GLV production in plants." The scientists made
3-D images of the enzymes, which allowed them to make a small,
but specific, genetic change in AOS, leading to the generation of
HPL. AOS and HPL are part of a super family of enzymes called
cytochrome P450. P450 family enzymes are found in most bacteria
and all known plants and animals. Although AOS or HPL are not
found in humans, there are related P450 family members that help
metabolize nearly half of the pharmaceuticals currently in use.
In plants, AOS and HPL break down naturally-occurring , organic
peroxides into GLV and jasmonate molecules. "Each flavor has a
different chemical profile," Raman said. "A notable strength of
this manuscript is the combined use of structural and
evolutionary biology to draw new insights regarding enzyme
function. These insights led to the striking demonstration that a
single amino acid substitution converts one enzyme into another,
thereby showing how a single point mutation can contribute to the
evolution of different biosynthetic pathways. This begins to
answer the long-standing question as to how the same starting
molecule can be converted into different products by enzymes that
look strikingly similar," said Rodney E. Kellems, Ph.D.,
professor and chairman of the Department of Biochemistry &
Molecular Biology at the UT Medical School at Houston. The study
dispels the earlier view that these flavor-producing enzymes are
only found in plants, Raman said. "We have discovered that they
are also present in marine animals, such as sea anemone and
corals. However, we do not know what they do in these organisms."
The lead authors were Dong-Sun Lee, Ph.D., an assistant professor
in the Department of Biochemistry & Molecular Biology at the UT
Medical School at Houston, and Pierre Nioche, Ph.D., an assistant
professor at the Universit=C3=A9 Paris Descartes. Mats Hamberg,
M.D., Ph.D., professor of medical chemistry in the Division of
Physiological Chemistry, Karolinska Institutet, Stockholm,
Sweden, collaborated on the research. The research is sup****ted
by Pew Charitable Trusts through a Pew Scholar Award, The Robert
A. Welch Foundation, The National Institutes of Health, a
Beginning Grant in Aid from the American Heart Association, and
an INSERM Avenir Grant sponsored by La Fondation pour la
Recherche Medicale. Journal reference: 1. Lee et al.
Structural insights into the evolutionary paths of oxylipin
biosynthetic enzymes. Nature, 2008; DOI: 10.1038/nature07307
Adapted from materials provided by University of Texas Health
Science Center at Houston.
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