Making enzymes from proteins
Computational design transforms protein without catalytic properties into an
active enzyme
By Charles Q Choi

Using computational design, researchers have transformed a protein with no
catalytic abilities into a highly active enzyme. Scientists said the
experiment, reported in the June 25 Science, represents a valuable step in
the quest to design enzymes from scratch.

"In principle, the design tools are general and may be used to design many
different enzymes at will. If this turns out to be true, then we can really
start to design catalysts at will," Homme Hellinga at Duke University
Medical Center in Durham, NC, senior author on the paper, told The
Scientist.

Hellinga and his team began with ribose-binding protein (RBP), a molecule
they had in prior computational biology experiments made into a
high-affinity receptor for nonnatural ligands such as serotonin and
trinitrotoluene. Their latest research transformed RBP into an enzyme highly
active as a triose phosphate isomerase (TIM). TIM is active in glycolysis,
catalyzing the interconversion between the ketose dihydroxyacetone phosphate
(DHAP) and the aldose glyceraldehyde-3-phosphate (GAP).

"This is really the best demonstration to date that these algorithms can be
useful for real practical problems and also for providing fundamental
insight into how enzymes do what they do," said Bill DeGrado at the
University of Pennsylvania School of Medicine in Philadelphia, who was not
involved in the study.

Read the rest at The Scientist
http://www.biomedcentral.com/news/20040625/01

Posted by
Robert Karl Stonjek.
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