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Lesa Beamer, PhD, and Steven Van Doren, PhD, use MU's 800 MHz NMR spectrometer, the second of its generation in the U.S. and the only one in Missouri, for their enzyme research.


Biochemists Peer into Enzyme that Makes Bacteria Hazardous to Patients


New $1.04 million grant and large NMR spectrometer support chemical reaction research

Scientists know that enzymes function as catalysts for chemical reactions, but much about the internal machinery of enzymes remains a mystery. Now, a $1.04 million grant from the National Science Foundation will help MU biochemists Lesa Beamer, PhD, and Steven Van Doren, PhD, explore the pathways and networks in one enzyme that could play a role in preventing bacteria from infecting patients with weakened immune systems.

"We have known for a long time that enzymes are complicated, but studying their complexity has been difficult because the technology wasn't available until now," said Beamer, an associate professor of biochemistry. "Thanks to MU's recent investment in scientific resources, we have all of the right tools here to study the movements of these enzymes, as well as to attract external grant funding for our research."

Using a $2.1 million nuclear magnetic resonance (NMR) spectrometer installed at MU in 2008, Beamer and Van Doren hope to generate new insights about the internal functions of the phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme as it interacts with sugar molecules. The second of its generation installed in the U.S. and the only one in Missouri, MU's 800-megahertz NMR spectrometer offers one of only a few methods available for examining the three-dimensional structure of molecules. The NMR is in a $10 million medical research building that opened two years ago.

Beamer and Van Doren's research findings could aid in the development of new types of antibiotics, since the enzyme being studied, PMM/PGM, is produced by the bacteria Pseudomonas aeruginosa. The bacteria can grow in the body, in soil and on multiple surfaces and can cause severe infections in patients with underlying medical problems like cystic fibrosis.

"If scientists have a better understanding of this enzyme, then there's a better possibility of building a drug to stop the enzyme from working," said Van Doren, a professor of biochemistry. "The bacteria uses the enzyme in a pathway to create a system of defense, so if the enzyme can't work, then bacteria could be easier to eradicate in a clinical setting."

Beamer and Van Doren's study of how enzyme structures move and fluctuate, and how the timing of such activity affects an enzyme chemical reaction, is regarded as a promising new area of research.

"Our peers are calling this research transformative, and we are encouraged by that designation," Beamer said. "We believe that our research, using this level of detail, could change the way we think about not only this protein but also other enzymes and their biological systems."

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