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Biological Chemistry

Single mutation transforms enzyme's function

August 28, 2006 | A version of this story appeared in Volume 84, Issue 35

By making a single amino acid change in an enzyme, researchers have completely changed the class of reaction catalyzed by that enzyme. Guided by the predicted mechanism of action of arylmalonate decarboxylase, Hiromichi Ohta and coworkers at Keio University, Yokohama, Japan, find that mutation of one residue in the enzyme converts its catalytic activity from enantioselective decarboxylation of α-aryl-α-methylmalonates to racemization of α-arylpropionates (Chem. Commun. 2006, 3600). This is not the first time an enzyme's activity has been modified by a single amino acid change. But Per Berglund of Sweden's Royal Institute of Technology, in Stockholm, who carried out one of the earlier efforts, says the Japanese study "is still an extremely nice example of creating a new activity in an enzyme by carefully studying the reaction mechanism." He notes that such changes usually involve reinforcing an enzyme's existing side reaction, while this study shows that the capability for the new reaction does not have to be present at all in the parent enzyme.

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