A research team at Iowa State has discovered a unique enzyme that can help scientists study the function and production of carbohydrates.

This enzyme is special because it can combine with numerous substrates, or chemical substances, to create many different non-natural sugars, unlike most enzymes that can only combine with one substrate.

Nicola Pohl, assistant professor of chemistry and member of the ISU Plant Sciences Institute, presented her team’s findings at the Biophysical Society Annual Meeting in Long Beach, Calif., from Feb. 12 to 16.

She said that, after she explained her findings, “people didn’t know what to make of it.” But after her presentation, she said, people came up to her — including representatives of some biotechnology companies — who were very interested in the research.

The enzyme in the study came from deep-sea archaea, Pohl said. Archaea is one of the three major branches of life recognized today, along with eukaryotes (plants and humans) and bacteria. The distinct properties of the single-cell archaea were not recognized until 1976, Pohl said.

The study was the first to look at an enzyme from an archaeal source.

“Archaea is everywhere,” Pohl said. “It is in the gut linings of humans and animals — it is even found in the soil.”

One reason this team set out in 2000 to study carbohydrates is because understanding of carbohydrate function and production is limited.

Pohl said many people think of carbohydrates as an energy source; however, she said, there is much more to it.

“One percent of the proteins in the body make sugar, but we don’t know what they do,” she said. “We are trying to make this easier.”

The four members of the team were Pohl, Rahman Mizanur, Corbin Zea and Firoz Jaipuri. Mizanur is a postdoctoral researcher, and Zea and Jaipuri are graduate students in chemistry.

Zea said one nice thing about working with this enzyme is that the hot temperature at which it is found aids in producing faster chemical reactions.

“It is easier to heat something up than to cool it down,” Zea said.

Not only did the team find a stable enzyme, Zea said, it also found a “promiscuous” enzyme. For example, he said, a typical enzyme will accept one substrate, but this enzyme will accept five or more substrates, and each of these enzyme-substrate combinations produces a carbohydrate with a different molecular structure.

The second half of the finding, Pohl said, stems from using the enzyme as a tool. She said each cell has many carbohydrates attached to its outside, and this enzyme can help study what makes these carbohydrate “forests.”

Without the enzyme, which acts as a handle to get a hold of the carbohydrates on the outside of the cell, it is impossible to study the enzymes that hold these sugars together, Pohl said.

Jaipuri said this finding will also make it possible to produce the sugars that are often used by viruses and bacteria that cause disease and infection.

Pohl said those viruses and bacteria also use their sugary outsides to attach to human tissues or to evade the human immune systems.

The plans of the researchers who have contacted Pohl are confidential, she said.

In general, she said, they will use the enzyme to make non-natural sugars to help them study the function of carbohydrates in a cell, and then they will use this information to develop vaccines and drugs that will interfere with the processes that cause disease.