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
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Posted by Robert Karl Stonjek.