UA Researcher Wins American Chemical Society Award

UA Researcher Wins American Chemical Society Award

By Rebecca Ruiz-McGill
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Vahe Bandarian
Vahe Bandarian

University of Arizona researcher Vahe Bandarian is the 2010 recipient of the Pfizer Award in Enzyme Chemistry from the American Chemical Society Division of Biological Chemistry.

The award – established in 1945 and consisting of a gold medal and honorarium – is given to stimulate fundamental research in enzyme chemistry by scientists who are 40 or younger.

The 39-year-old Bandarian, associate professor with the department of chemistry and biochemistry, was recognized for his research, which uses the tools of chemistry and of biology to elucidate the biosynthetic pathways by which deazapurine-containing metabolites are produced.

The work has the potential to help lead to cures for a variety of human diseases.

Deazapurines are secondary metabolites that are derived from purines – one of the two constituents of DNA – and little is known about how they are synthesized in the cell.

An understanding of how cells synthesize and regulate the production of secondary metabolites can enable researchers in the development of human therapeutic agents.

These secondary metabolites and their diverse biological functions have led to cures for human diseases through the development of hormones, antibiotics, antitumor agents and antivirals. 

Bandarian and his colleagues have undertaken studies with an eye toward understanding the pathways and chemical transformations that underlie the biosynthesis of these metabolites, the mechanisms for the evolution of catalysts in these pathways, and the broader issues involving the evolution of secondary metabolic pathways.

"We are interested in how bacteria make compounds that have drug-like properties. Bacteria make large secondary metabolites, which, while not required for primary metabolic processes, confer selective advantage to the producer and allow survival in complex biological systems. If we understand how the secondary molecules are synthesized, then perhaps the cellular machinery can be co-opted to synthesize new compounds with more desirable therapeutic spectra," Bandarian said.

In presenting Bandarian with the award, the society noted him for the identification and characterization of the gene cluster responsible for the production of the deazapurine natural products toyocamycin and sangivamycin, both antibiotics in the soil bactirium Streptomyces rimosus.

Although this class of compounds was discovered more than four decades ago, the biosynthetic pathways that produced them had remained elusive.

Bandarian also was recognized for applying contemporary technology and careful molecular logic to clone, in a test tube, the genes for the production of 7-deaza-7-cyanoguanine (also known as preQ0), the modified base in these antibiotics. 

In addition to identifying the enzymes responsible for the production of preQ0, Bandarian and his colleagues have explored a range of problems in deazapurine production.

In announcing the award, the American Chemical Society said Bandarian's work was a tour de force at the cutting edge of microbial bioinformatics. They added that the set of publications describing the reconstitution of the synthesis of preQ0 in vitro is transformative in that it opens this field of biosynthesis and sets the stage for detailed studies of these enzymes and the reactions they catalyze. In addition, the society said, the broader evolutionary questions that Bandarian poses will no doubt provide new surprises with equally rich biochemistry to be explored.

There have been 65 previous Pfizer Award in Enzyme Chemistry winners, including 1976 awardees Michael S. Brown and Joseph L. Goldstein, who went on to win the Nobel Prize in 1986 for their work in the regulation of cholesterol metabolism.

"It's an honor to receive the award. I'm humbled to be included in that list of scientists whom I respect and whose work I have admired," Bandarian said.

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