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Biological Chemistry

Enzyme activity: Out with the old, in with the new

January 30, 2006 | A version of this story appeared in Volume 84, Issue 5

Mimicking the natural process of evolution, researchers have redesigned a natural enzyme, thereby causing it to lose its original activity and adopt a new one (Science 2006, 311, 535). Hak-Sung Kim of the Korea Advanced Institute of Science & Technology, Daejon, South Korea, and coworkers started with a core structure of the enzyme glyoxalase II that has thiolester hydrolysis activity. They subjected the protein to an approach called SIAFE (simultaneous incorporation and adjustment of functional elements) in conjunction with directed evolution (iterative modification and selection for desirable activity). The result was evMBL8, a designed enzyme with the ability to hydrolyze β-lactam amide bonds, a type of activity on which bacterial resistance to β-lactam antibiotics is based. Key to the change was the replacement of several of the enzyme's surface loop structures. The researchers say they hope the technique can be extended to convert other structures into enzymes that catalyze diverse reactions, including some not found in nature.

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