Scientists report unusual enzyme structure

June 10, 2009 at 4:12 PM
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CHAMPAIGN, Ill., June 10 (UPI) -- U.S. scientists have discovered the structure of an unusual enzyme that can break the bond between two carbon atoms in a single step.

University of Illinois researchers said their findings might help determine how bacteria develop resistance to new drugs and how to create drugs that overcome that resistance.

The scientists said they have, for the first time, described the three-dimensional structure of hydroxyethylphosphonate dioxygenase and proposed a mechanism by which the enzyme causes chemical reactions. The enzyme catalyzes a critical step in the production of phosphinothricin, a compound that is widely used as an agricultural herbicide.

"Our team discovered this very implausible chemical reaction," said Professor Wilfred van der Donk. "And the more we learned about it the more unusual it became. The enzyme is unusual because it breaks a carbon-carbon bond without needing anything except oxygen."

The researchers said their findings result from an ongoing study of molecules containing carbon-phosphorus bonds. Compounds using such molecules inhibit cellular processes in bacteria or other organisms and are used in agriculture and medicine.

Those compounds, van der Donk said, are candidates for the development of new antibiotics.

The study, which included Professor William Metcalf, appears in the journal Nature.

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