Research May Allow Enzyme’s to Fulfill Their Role in Disease

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Based on a recent study, a UT Arlington chemist doing National Science Foundation-funded research on enzymes that standardize human biology has discovered certain traits and qualities that could be used to distinguish predisposition to conditions such as heart disease, diabetic ulcers and some types of cancer.

Assistant professor of chemistry/biochemistry at The University of Texas at Arlington, Brad Pierce, assembled and led a team of researchers that studied and analyzed an oxygen utilizing iron enzyme called cysteine dioxygenase or CDO, which is located in high levels within the heart, liver, and brain tissues. Enzymes are proteins that serve as catalysts to allow metabolic functions, however, under certain circumstances these oxygen-dependent enzymes can also generate highly toxic side products known as reactive oxygen species or ROS.

For the very first time, Pierce's team discovered that mutations outside the CDO active site setting or "outer coordination sphere" have a significant impact on the release of ROS. Surplus ROS has been tied to several age-onset human disease states.

"Most research in the past has focused on the active site inner coordination sphere of these enzymes, where the metal molecule is located. What we're finding is that it's really the second sphere that regulates the efficiency of the enzyme. In essence, these interactions hold everything together during catalysis. When this process breaks down, the enzyme ends up spitting out high levels of ROS and increasing the likelihood of disease,” said Pierce.

Pierce trusts that the team’s findings from the CDO enzyme could be implemented into other oxygen-dependent enzymes, which constitute of up to about 20 percent of the enzymes in the human body.

"In principle, these findings could be extended to better understand how other enzymes within the class generate ROS and potentially be used to screen for genetic dispositions for ROS-related diseases," he said.

Pierce's research introduces a whole new level of detail to enzyme study through the use of electron paramagnetic resonance or EPR, a technology that very much resembles the magnetic resonance imaging or MRI used in the medical field. In fall 2012, the National Science Foundation awarded Pierce a three-year, $300,000 grant to study enzymes that are catalysts for the oxidation of sulfur-bearing molecules in the body.

"Dr. Pierce's research is a good example of how basic science can set a path toward discoveries that affect human health. We look forward to his continued exploration of these findings," said dean of the UT Arlington College of Science, Pamela Jansma.

The study was published by the American Chemical Society journal Biochemistry. Pierce is registered as the corresponding author on the paper, with UT Arlington students Wei Li, Michael D. Pecore and Joshua K. Crowell as co-authors. Co-author Elizabeth J. Blaesi is a graduate research assistant at the University of Wisconsin.

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