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Scientists reveal structural secrets of enzyme used to make popular anti-cholesterol drug
Date:5/13/2014

and located at the Pittsburgh Supercomputing Center.

"In the machines that we have for our routine calculations, each of the simulations in this timescale takes more than one month," Jimnez-Oss said. "Using Anton, we can do the same amount of calculations in one day. It is a huge improvement."

From the results of their computer simulations, Houk and Jimnez-Oss determined that part of what makes the mutated enzyme so effective is that it can function without the involvement of an additional protein that is required by the natural enzyme. Also, the mutated enzyme moves and twists in such a way that it remains in a configuration beneficial for simvastatin production far more often than its natural counterpart.

These calculations enabled the research team to understand how mutations located far from the active part of the enzyme can improve its performance.

"The directed evolution changes the nature of the amino acids that are in the protein," Houk said. "The molecular dynamics simulations allowed us to trace how these changes in amino acids altered the structure of the protein and made it appropriate for use as a catalyst."

In the case of LovD9, these small differences make the reaction to manufacture simvastatin vastly more efficient. Now that they know which structural features in the mutated enzyme help improve simvastatin production, the team hopes to directly engineer an enzyme with similar properties without resorting to the more random directed evolution process.

"What was special about this study is that we analyzed what happened during directed evolution in order to try to understand how these improvements are made within the protein," Yeates said. "We hope in the future that it might be possible to make better enzymes in rational ways by understanding how it occurs in random ways."

The mystery behind the mutated LovD9 enzyme may have remained unsolved without an extraordinary degree of collaborati
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Contact: Stuart Wolpert
swolpert@support.ucla.edu
310-206-0511
University of California - Los Angeles
Source:Eurekalert  

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