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Virginia Tech researcher to examine enzymes to improve human health

AFP

vtech-logoA Virginia Tech researcher has received a $480,000 National Science Foundation (NSF) grant to study a group of enzymes with potential human health benefits.

Pablo Sobrado, an associate professor of biochemistry in the College of Agriculture and Life Sciences and a Fralin Life Science Institute affiliate at Virginia Tech, studies the function of flavin-dependent enzymes, which are involved in many biochemical reactions in the cell.

In particular, he and his research team study enzymes that catalyze unique chemical reactions that are essential for microbial survival but are absent in humans.

One of these enzymes, UDP-galactopyranose mutase, is involved in helping the bacteria that causes tuberculosis infect its human host. Understanding more about its structure and function could lead to improved treatment, according to Sobrado, who is also affiliated with the Virginia Tech Center for Drug Discovery.

One third of the world’s population is infected with tuberculosis, and in 2013, 1.5 million people died because of tuberculosis-related causes, according to the Centers for Disease Control and Prevention.

Another enzyme that Sobrado studies, 2-haloacrylate hydratase, has properties that could be useful in cleaning up chemical pollutant spills. Recently, his group determined that 2-haloacrylate hydratase can deactivate halogenated hydrocarbons — compounds extensively used in industrial processes and agricultural pesticides that have been found to be toxic and linked to ozone deterioration.

With the new grant, the Sobrado team will explore the function of these enzymes and others to improve human health. Virginia Tech will conduct the project with the University of Missouri, in the laboratory of John Tanner, a professor of biochemistry and the co-principal investigator on the grant.

“Our investigation will provide detailed information about the function of unique flavoenzymes,” said Sobrado. “This information can be used for drug design or protein engineering.”




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AFP

AFP

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